|
Name |
Accession |
Description |
Interval |
E-value |
| GPS2_interact |
pfam15784 |
G-protein pathway suppressor 2-interacting domain; GPS2_interact is the more N-terminal domain ... |
392-480 |
1.88e-33 |
|
G-protein pathway suppressor 2-interacting domain; GPS2_interact is the more N-terminal domain of two co-repressor protein-families found in vertebrates. The domain is found in NCoR and SMRT proteins; N-CoR (nuclear receptor co-repressor) and SMRT (silencing mediator for retinoid and thyroid receptors) are related corepressors that mediate transcriptional repression by unliganded nuclear receptors and other classes of transcriptional repressors. GPS2 is a stoichiometric subunit of the N-CoR-HDAC3 complex. GPS2 links the complex to membrane receptor-related intracellular JNK (c-Jun amino-terminal kinase) signalling pathways.
Pssm-ID: 464868 [Multi-domain] Cd Length: 89 Bit Score: 124.97 E-value: 1.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 392 YTPQTEAISPTLPEPNTQEDAL---RSTKDELLQQIGKVDREIAKRENQLNMLRKRIKELEEAANKPleaTGLKRNIEEQ 468
Cdd:pfam15784 1 YYPQVEAISPTLPSPEGQDQELspfRSSKDELLQNIDKVDREIAKVEQQISKLKKKQQQLEEEAAKP---PEPEEPVSPP 77
|
90
....*....|..
gi 1418074753 469 SQQPKHQSLAQK 480
Cdd:pfam15784 78 PSESKHRSLAQI 89
|
|
| Myb_DNA-binding |
pfam00249 |
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ... |
1158-1201 |
1.19e-12 |
|
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.
Pssm-ID: 459731 [Multi-domain] Cd Length: 46 Bit Score: 64.06 E-value: 1.19e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1418074753 1158 PWTDEELEQLRKALREYGTNWPKIAEQIPGKTSQQCKNYYFAYR 1201
Cdd:pfam00249 3 PWTPEEDELLLEAVEKLGNRWKKIAKLLPGRTDNQCKNRWQNYL 46
|
|
| SANT |
cd00167 |
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ... |
1158-1200 |
4.83e-12 |
|
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.
Pssm-ID: 238096 [Multi-domain] Cd Length: 45 Bit Score: 62.59 E-value: 4.83e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1418074753 1158 PWTDEELEQLRKALREYGT-NWPKIAEQIPGKTSQQCKNYYFAY 1200
Cdd:cd00167 1 PWTEEEDELLLEAVKKYGKnNWEKIAKELPGRTPKQCRERWRNL 44
|
|
| SANT |
smart00717 |
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains; |
1157-1203 |
1.63e-11 |
|
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
Pssm-ID: 197842 [Multi-domain] Cd Length: 49 Bit Score: 61.09 E-value: 1.63e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1418074753 1157 RPWTDEELEQLRKALREYGT-NWPKIAEQIPGKTSQQCKNYYFAYRKK 1203
Cdd:smart00717 2 GEWTEEEDELLIELVKKYGKnNWEKIAKELPGRTAEQCRERWRNLLKP 49
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1922-2097 |
4.42e-11 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 66.87 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1922 REQEIRMQEHRMAEhrltqqhQRERERERDIVHLREKEEHRLHREKELQQQLEhrlavQQHHQHREKDFQQQEHRLAPQR 2001
Cdd:pfam13868 34 IKAEEKEEERRLDE-------MMEEERERALEEEEEKEEERKEERKRYRQELE-----EQIEEREQKRQEEYEEKLQERE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 2002 EKDIHVEHARLQIREKdipHEHRLIHQQREKEIHQQIAAQR----------EKEHEHRLA-----VQQREKEIQHQEQRL 2066
Cdd:pfam13868 102 QMDEIVERIQEEDQAE---AEEKLEKQRQLREEIDEFNEEQaewkelekeeEREEDERILeylkeKAEREEEREAEREEI 178
|
170 180 190
....*....|....*....|....*....|.
gi 1418074753 2067 AIQQQRENphvvgSPIQQHAERLAAQQRERD 2097
Cdd:pfam13868 179 EEEKEREI-----ARLRAQQEKAQDEKAERD 204
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1917-2094 |
7.89e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 7.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1917 NNRAFREQEIRMQEHRMAEHRLTQQHQRERERERDIVHLREKEEHRLHREKELQQQLEHRLAVQQHHQHREK--DFQQQ- 1993
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElaELPERl 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1994 ---EHRLAPQREKDIHVEHARLQIREKDipHEHRLIHQQREKEIHQQIAAQREKEHEHRLAVQQREKEIQHQEQRLAIQQ 2070
Cdd:COG4717 149 eelEERLEELRELEEELEELEAELAELQ--EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180
....*....|....*....|....
gi 1418074753 2071 QRENPHVVGSPIQQHAERLAAQQR 2094
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARL 250
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
407-628 |
3.72e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 407 NTQEDALRSTKDELLQQIGKVDREIAKRENQLNMLRKRIKELEEAANKpleatgLKRNIEEQSQQPKHQslaQKIYAENR 486
Cdd:COG4942 40 EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE------LEKEIAELRAELEAQ---KEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 487 RKAEEAHRLmeklgPKIELPLYNQPSDTSVYQENRTRHQTCMRTRLIARLRRDHTERASLHQQQTQTYTILVQewhrKVE 566
Cdd:COG4942 111 RALYRLGRQ-----PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA----LLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1418074753 567 RLEATQKRKSKETKNReffEKVFPELRKQREDKERfnRVGARIKSEADLEEIMDGLQEQEEE 628
Cdd:COG4942 182 ELEEERAALEALKAER---QKLLARLEKELAELAA--ELAELQQEAEELEALIARLEAEAAA 238
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1914-2092 |
2.06e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 56.26 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1914 RYDNNRAFREQEIRMQEHRMAEHRLTQQHQRERERERDIvhlREKEEHRLHREKELQQQLEHRLAVQQHHQ-HREKDFQQ 1992
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRE---RNQQRQEARREREELQREEERLVQKEEQLdARAEKLDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1993 QEHRLApQREKDIHVEHARLQIREKDIPHEHRLIHQQREKEIHQQIAAQREKEHEHRLAVqqrekEIQHQEQRLAIQQQR 2072
Cdd:PRK12705 103 LENQLE-EREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQ-----RVKKIEEEADLEAER 176
|
170 180
....*....|....*....|
gi 1418074753 2073 ENPHVVGSPIQQHAERLAAQ 2092
Cdd:PRK12705 177 KAQNILAQAMQRIASETASD 196
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
412-646 |
1.72e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 412 ALRSTKDELLQQIGKVDREIAKRENQLNMLRKRIKELE---EAANKPLEATG------LKRNIEEQSQQpkhQSLAQKIY 482
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEqllEELNKKIKDLGeeeqlrVKEKIGELEAE---IASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 483 AENRRKAEEAHRLMEKLGPKIE-LPLYNQPSDTSVYQENRTRHQtcmrtrLIARLRRDHTERASLH---QQQTQTYTILV 558
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDkLLAEIEELEREIEEERKRRDK------LTEEYAELKEELEDLRaelEEVDKEFAETR 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 559 QEWHRKVERLEATQKRKSKETKNReffEKVFPELRKQREDKERFNRVGARIKS-----EADLEEIMDGLQEQEE--ETLQ 631
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKREL---DRLQEELQRLSEELADLNAAIAGIEAkinelEEEKEDKALEIKKQEWklEQLA 461
|
250
....*....|....*
gi 1418074753 632 DLKNSIKAcQLEDKK 646
Cdd:TIGR02169 462 ADLSKYEQ-ELYDLK 475
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1383-1689 |
2.66e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.40 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1383 PPTTAHSPPSTTSNSNPLTVKDLMLGVIEMQLKRTPNSPADGGGSSAPNSSGTPTISSILKTDHRNDI----------TY 1452
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPpaapaagpprRL 2783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1453 VRGYKSSSNMTNTALPSRDTNLATLSVVSGPHHGHRSAPSPQQISQMQATITPCPPAAPSnqGSSSDLLPKEGLVVMQVQ 1532
Cdd:PHA03247 2784 TRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP--GPPPPSLPLGGSVAPGGD 2861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1533 QALRETEGTLDLSIKKPRlqqdynhsiqlhKPPTVTLYRPEPPPGAYYHPHTTPHPEQGRNAKSPLVYASAPRPQASITP 1612
Cdd:PHA03247 2862 VRRRPPSRSPAAKPAAPA------------RPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQP 2929
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1418074753 1613 KMNKVTVPQTHPKLSPKLGSMSTPGHKGGSITHGTPVSTARYEGLLRQMTPPGNPPVSGASANVSERGGGAVNASSA 1689
Cdd:PHA03247 2930 QPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSS 3006
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1906-2095 |
3.83e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1906 MADRLlaDRYDNNRAFREQEIRMQEHRMAEHR--LTQQHQRERERERDIVHLREKEEHRLHREKELQQQL----EHRLAV 1979
Cdd:TIGR02169 679 LRERL--EGLKRELSSLQSELRRIENRLDELSqeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLssleQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1980 QQHHQHREKDFQQQEHRLAPQREK--DIHVEHARLQIREKDipHEHRLIHQQReKEIHQQIAAQREKEHEHRLAVQQREK 2057
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEAlnDLEARLSHSRIPEIQ--AELSKLEEEV-SRIEARLREIEQKLNRLTLEKEYLEK 833
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1418074753 2058 EIQH--------QEQRLAIQQQRENPHVVGSPIQQHAERLAAQQRE 2095
Cdd:TIGR02169 834 EIQElqeqridlKEQIKSIEKEIENLNGKKEELEEELEELEAALRD 879
|
|
| Activator_LAG-3 |
pfam11498 |
Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of ... |
1775-2048 |
5.99e-06 |
|
Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of growth, differentiation and patterning in animal development, relies on either of the receptors GLP-1 or LIN-12. Both these receptors promote signalling by the recruitment of LAG-3 to target promoters, where it then acts as a transcriptional activator. LAG-3 works as a ternary complex together with the DNA binding protein, LAG-1. Its N-terminal region adopts an elongated kinked helix that is required for complex assembly.
Pssm-ID: 151935 [Multi-domain] Cd Length: 476 Bit Score: 51.50 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1775 PSYTMEQQLSSRQ---IIM----NDYITSQQMHARARGSGSTGA--SVTGEMASKNEPPPSNLYYASTPPPPPPQTHTQP 1845
Cdd:pfam11498 157 PQFQMQQQYHSQQqqyIMMaaqhHHFMGMQQIHHQMPSTSSADAihSVPTPAGSIHQPSPAEMQNGCGMSRNATMDMTCS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1846 RQGVIQRHNPQKQMHYPPPPILDAFSNLVEVAIKQPTLPVPHQHGHPPSGSGGHEGLGKTMADRLLADRYDNNR-----A 1920
Cdd:pfam11498 237 PMSGGLPISDENNLAVPEGEWFDKLALAVAEKYDADTILGPDTYDTFLAELDAMEPEGETKKSPMEAGGDRMPQsapppA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1921 FREQEIRMQEHRMAEHRLTQQHQR-----ERERERDIVHLREKEEHRLHREKEL---QQQLEHRLavQQHHQ-HREKDFQ 1991
Cdd:pfam11498 317 MNPQHIAQLAQQQNKMRLLQQQEMemqriEQQRQQQIMHQHQQQQQQEHQQQQMllqQQQQMHQL--QQHHQmNGGGQFA 394
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1418074753 1992 QQEHRLAPQREKdihVEHARLQIREKdiphehrliHQQREKEIHQQIAAQREKEHEH 2048
Cdd:pfam11498 395 TQAHQHAAYLQQ---MQHMRLQEQIQ---------HQQQQAQHHQQAQQQHQQPAQH 439
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
412-705 |
2.76e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 412 ALRSTKDELLQQIGKVDREIAKRENQLNMLRKRIKELEEAANKPLEATGLKRNIEEQSQ--QPKHqslaqKIYAENRRKA 489
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEelEERH-----ELYEEAKAKK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 490 EEAHRLMEKLGP----KIElplynqpsdtSVYQENRTRHQTCMRTR--LIARLRRDHTERASL----------------- 546
Cdd:PRK03918 372 EELERLKKRLTGltpeKLE----------KELEELEKAKEEIEEEIskITARIGELKKEIKELkkaieelkkakgkcpvc 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 547 -------HQQQtqtytiLVQEWHRKVERLEATQKR-KSKETKNREFFEKV------FPELRKQREDKERFNRVGARIKsE 612
Cdd:PRK03918 442 grelteeHRKE------LLEEYTAELKRIEKELKEiEEKERKLRKELRELekvlkkESELIKLKELAEQLKELEEKLK-K 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 613 ADLEEIMDGLQEQEE--ETLQDLKNSIKACQLEDKKMRSYavippllldaKQRRIAFQNRNGLLQpEELEALHseRKLIN 690
Cdd:PRK03918 515 YNLEELEKKAEEYEKlkEKLIKLKGEIKSLKKELEKLEEL----------KKKLAELEKKLDELE-EELAELL--KELEE 581
|
330 340
....*....|....*....|....
gi 1418074753 691 V-WSSVEH--------ESFKEKYL 705
Cdd:PRK03918 582 LgFESVEEleerlkelEPFYNEYL 605
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1427-1885 |
5.72e-05 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 48.76 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1427 SSAPNSSGT-PTISSIlktdhrndityvrGYKSSSnmTNTALPSRD---TNLaTLSVVSGP--HHGHRSAPSPQQISQMQ 1500
Cdd:pfam05109 422 SKAPESTTTsPTLNTT-------------GFAAPN--TTTGLPSSThvpTNL-TAPASTGPtvSTADVTSPTPAGTTSGA 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1501 ATITPCPpaAPSNQGSSS---DLLPKEGLVVMQVQQAlreTEGTLDLSIKKPrlqqdynhsiqlhKPPTVTLYRPEPPPG 1577
Cdd:pfam05109 486 SPVTPSP--SPRDNGTESkapDMTSPTSAVTTPTPNA---TSPTPAVTTPTP-------------NATSPTLGKTSPTSA 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1578 AyyhphTTPHPeqgrNAKSPLVYASAPRPQASI-----TPKMNKVTVPqTHPKLSPKLGSMS----TPGHKGGSiTHGTP 1648
Cdd:pfam05109 548 V-----TTPTP----NATSPTPAVTTPTPNATIptlgkTSPTSAVTTP-TPNATSPTVGETSpqanTTNHTLGG-TSSTP 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1649 VSTARYEGLLRQMTPPGNPPVSGASANVSERGGG---------AVNASSAGP--GAPKETGGGSITQGTPVLPfavdkrg 1717
Cdd:pfam05109 617 VVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSisetlspstSDNSTSHMPllTSAHPTGGENITQVTPAST------- 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1718 apiyDYHRTIRHSPVTGSGNVPPPPGQGPPSQATSPAVVVSHGGSqynsysaagrpPPSYTMEQQLSSRQIIMNDYITSQ 1797
Cdd:pfam05109 690 ----STHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGT-----------PPKNATSPQAPSGQKTAVPTVTST 754
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1798 QMHArarGSGSTGASVTGEMASKNEPP----------PSNLYYASTPPPPPPQTHTQPRQGVIQRHNPQKQMHYPPPPIL 1867
Cdd:pfam05109 755 GGKA---NSTTGGKHTTGHGARTSTEPttdyggdsttPRTRYNATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPTS 831
|
490
....*....|....*....
gi 1418074753 1868 DA-FSNLVEVAIKQPTLPV 1885
Cdd:pfam05109 832 QPrFSNLSMLVLQWASLAV 850
|
|
| ClassIIa_HDAC4_Gln-rich-N |
cd10162 |
Glutamine-rich N-terminal helical domain of HDAC4, a Class IIa histone deacetylase; This ... |
1965-2050 |
3.01e-04 |
|
Glutamine-rich N-terminal helical domain of HDAC4, a Class IIa histone deacetylase; This family consists of the glutamine-rich domain of histone deacetylase 4 (HDAC4). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.
Pssm-ID: 197398 [Multi-domain] Cd Length: 90 Bit Score: 42.11 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1965 REKELQQQLehrLAVQQHHQHREK----DFQQQEHRLAPQREKDIHvEHARLQIREKDIPHEHRLIHQQREKEIHQQIAA 2040
Cdd:cd10162 5 REQQLQQEL---LALKQKQQIQRQlliaEFQRQHEQLSRQHEAQLH-EHIKQQQELLAMKHQQELLEHQRKLERHRQEQE 80
|
90
....*....|
gi 1418074753 2041 QREKEHEHRL 2050
Cdd:cd10162 81 MEKQQREQKL 90
|
|
| F-BAR_PombeCdc15_like |
cd07651 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ... |
411-637 |
2.92e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153335 [Multi-domain] Cd Length: 236 Bit Score: 41.90 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 411 DALRsTKDELL---QQIGKVDREIAKRENQLNmlRKRIKELEEaankpleaTGLKRN-----IEEQSQQPKHQSLAQKIY 482
Cdd:cd07651 16 DSLR-TLEELRsfyKERASIEEEYAKRLEKLS--RKSLGGSEE--------GGLKNSldtlrLETESMAKSHLKFAKQIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 483 AENRRKAEEAHRLMEKLGPKIEL---PLYNQPSDTSVY-QENRTRHQT-CMRTRliarlrrdhteraSLHQQQTQTytil 557
Cdd:cd07651 85 QDLEEKLAAFASSYTQKRKKIQShmeKLLKKKQDQEKYlEKAREKYEAdCSKIN-------------SYTLQSQLT---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 558 vqeWHRKVERLEA--TQKRKSKETKNREFFEKVfpelRKQREDKERFNRvgarikseaDLEEIMDGLQEQEEETLQDLKN 635
Cdd:cd07651 148 ---WGKELEKNNAklNKAQSSINSSRRDYQNAV----KALRELNEIWNR---------EWKAALDDFQDLEEERIQFLKS 211
|
..
gi 1418074753 636 SI 637
Cdd:cd07651 212 NC 213
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
407-499 |
3.05e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 407 NTQEDALRSTKDELLQQIGKVDREIAKRENQLNMLRKRIKELEEAANKPLEATGLKRN-IEEQSQQPKH--------QSL 477
Cdd:PRK12704 53 AIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEeLEKKEKELEQkqqelekkEEE 132
|
90 100 110
....*....|....*....|....*....|.
gi 1418074753 478 AQKIYAENRRK--------AEEA-HRLMEKL 499
Cdd:PRK12704 133 LEELIEEQLQElerisgltAEEAkEILLEKV 163
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
413-643 |
3.05e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 413 LRSTKDELLQQIGKVDREIAKRENQLNMLRKRIKelEEAANKpleATGLKRNIEEQSQQPKHQS-LAQKIYAenRRKAEE 491
Cdd:pfam01576 220 LQEQIAELQAQIAELRAQLAKKEEELQAALARLE--EETAQK---NNALKKIRELEAQISELQEdLESERAA--RNKAEK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 492 AHR-LMEKL-GPKIELPlyNQPSDTSVYQENRTRhqtcmRTRLIARLRRDHTERASLHQQQT----QTYTILVQEWHrkv 565
Cdd:pfam01576 293 QRRdLGEELeALKTELE--DTLDTTAAQQELRSK-----REQEVTELKKALEEETRSHEAQLqemrQKHTQALEELT--- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 566 ERLEATQKRKSKETKNREFFEKVFPELRKQ-------REDKERfnrvgARIKSEADLEEIMDGLQEQEEETlQDLKNSIK 638
Cdd:pfam01576 363 EQLEQAKRNKANLEKAKQALESENAELQAElrtlqqaKQDSEH-----KRKKLEGQLQELQARLSESERQR-AELAEKLS 436
|
....*
gi 1418074753 639 ACQLE 643
Cdd:pfam01576 437 KLQSE 441
|
|
| SANT_MTA3_like |
cd11661 |
Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family ... |
692-735 |
4.91e-03 |
|
Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family include domains found in mouse metastasis-associated protein 3 (MTA3) proteins and arginine-glutamic dipeptide (RERE) repeats proteins. SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domains are a diverse set of proteins that share a common 3 alpha-helix bundle. MTA3 has been shown to interact with nucleosome remodeling and deacetylase (NuRD) proteins CHD4 and HDAC1, and the core cohesin complex protein RAD21 in the ovary, and regulate G2/M progression in proliferating granulosa cells. RERE belongs to the atrophin family and has been identified as a nuclear receptor corepressor; altered expression levels of RERE are associated with cancer in humans while mutations of Rere in mice cause failure in closing the anterior neural tube and fusion of the telencephalic and optic vesicles during embryogenesis.
Pssm-ID: 212559 [Multi-domain] Cd Length: 46 Bit Score: 37.21 E-value: 4.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1418074753 692 WSSVEHESFKEKYLQHPKNYGVIAQS-LEHKGVQDCVHHYYLTKK 735
Cdd:cd11661 2 WSESEAKLFEEGLRKYGKDFHDIRQDfLPWKSVGELVEFYYMWKK 46
|
|
| REB1 |
COG5147 |
Myb superfamily proteins, including transcription factors and mRNA splicing factors ... |
1158-1197 |
7.95e-03 |
|
Myb superfamily proteins, including transcription factors and mRNA splicing factors [Transcription / RNA processing and modification / Cell division and chromosome partitioning];
Pssm-ID: 227476 [Multi-domain] Cd Length: 512 Bit Score: 41.31 E-value: 7.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1418074753 1158 PWTDEELEQLRKALREYGTNWPKIAEQIPGKTSQQCKNYY 1197
Cdd:COG5147 74 NWSEEEDEQLIDLDKELGTQWSTIADYKDRRTAQQCVERY 113
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GPS2_interact |
pfam15784 |
G-protein pathway suppressor 2-interacting domain; GPS2_interact is the more N-terminal domain ... |
392-480 |
1.88e-33 |
|
G-protein pathway suppressor 2-interacting domain; GPS2_interact is the more N-terminal domain of two co-repressor protein-families found in vertebrates. The domain is found in NCoR and SMRT proteins; N-CoR (nuclear receptor co-repressor) and SMRT (silencing mediator for retinoid and thyroid receptors) are related corepressors that mediate transcriptional repression by unliganded nuclear receptors and other classes of transcriptional repressors. GPS2 is a stoichiometric subunit of the N-CoR-HDAC3 complex. GPS2 links the complex to membrane receptor-related intracellular JNK (c-Jun amino-terminal kinase) signalling pathways.
Pssm-ID: 464868 [Multi-domain] Cd Length: 89 Bit Score: 124.97 E-value: 1.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 392 YTPQTEAISPTLPEPNTQEDAL---RSTKDELLQQIGKVDREIAKRENQLNMLRKRIKELEEAANKPleaTGLKRNIEEQ 468
Cdd:pfam15784 1 YYPQVEAISPTLPSPEGQDQELspfRSSKDELLQNIDKVDREIAKVEQQISKLKKKQQQLEEEAAKP---PEPEEPVSPP 77
|
90
....*....|..
gi 1418074753 469 SQQPKHQSLAQK 480
Cdd:pfam15784 78 PSESKHRSLAQI 89
|
|
| Myb_DNA-binding |
pfam00249 |
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ... |
1158-1201 |
1.19e-12 |
|
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.
Pssm-ID: 459731 [Multi-domain] Cd Length: 46 Bit Score: 64.06 E-value: 1.19e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1418074753 1158 PWTDEELEQLRKALREYGTNWPKIAEQIPGKTSQQCKNYYFAYR 1201
Cdd:pfam00249 3 PWTPEEDELLLEAVEKLGNRWKKIAKLLPGRTDNQCKNRWQNYL 46
|
|
| SANT |
cd00167 |
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ... |
1158-1200 |
4.83e-12 |
|
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.
Pssm-ID: 238096 [Multi-domain] Cd Length: 45 Bit Score: 62.59 E-value: 4.83e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1418074753 1158 PWTDEELEQLRKALREYGT-NWPKIAEQIPGKTSQQCKNYYFAY 1200
Cdd:cd00167 1 PWTEEEDELLLEAVKKYGKnNWEKIAKELPGRTPKQCRERWRNL 44
|
|
| SANT |
smart00717 |
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains; |
1157-1203 |
1.63e-11 |
|
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
Pssm-ID: 197842 [Multi-domain] Cd Length: 49 Bit Score: 61.09 E-value: 1.63e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1418074753 1157 RPWTDEELEQLRKALREYGT-NWPKIAEQIPGKTSQQCKNYYFAYRKK 1203
Cdd:smart00717 2 GEWTEEEDELLIELVKKYGKnNWEKIAKELPGRTAEQCRERWRNLLKP 49
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1922-2097 |
4.42e-11 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 66.87 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1922 REQEIRMQEHRMAEhrltqqhQRERERERDIVHLREKEEHRLHREKELQQQLEhrlavQQHHQHREKDFQQQEHRLAPQR 2001
Cdd:pfam13868 34 IKAEEKEEERRLDE-------MMEEERERALEEEEEKEEERKEERKRYRQELE-----EQIEEREQKRQEEYEEKLQERE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 2002 EKDIHVEHARLQIREKdipHEHRLIHQQREKEIHQQIAAQR----------EKEHEHRLA-----VQQREKEIQHQEQRL 2066
Cdd:pfam13868 102 QMDEIVERIQEEDQAE---AEEKLEKQRQLREEIDEFNEEQaewkelekeeEREEDERILeylkeKAEREEEREAEREEI 178
|
170 180 190
....*....|....*....|....*....|.
gi 1418074753 2067 AIQQQRENphvvgSPIQQHAERLAAQQRERD 2097
Cdd:pfam13868 179 EEEKEREI-----ARLRAQQEKAQDEKAERD 204
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1909-2072 |
6.82e-10 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 63.40 E-value: 6.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1909 RLLADRYDNNRAFREQEIRMQEHRMAEHRLTQQHQRERERERDIVHL-REKEEH-RLHREKELQQQLEHRLAVQQHHQHR 1986
Cdd:pfam13868 162 KEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAkLYQEEQeRKERQKEREEAEKKARQRQELQQAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1987 EKDFQQQEHRLAPQREKD------IHVEHARLQIREKDIPHEHRLIHQQREKEIHQQI-------AAQREKEHEHRLAVQ 2053
Cdd:pfam13868 242 EEQIELKERRLAEEAEREeeeferMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIeereeqrAAEREEELEEGERLR 321
|
170
....*....|....*....
gi 1418074753 2054 QREKEiqhQEQRLAIQQQR 2072
Cdd:pfam13868 322 EEEAE---RRERIEEERQK 337
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1917-2094 |
7.89e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 7.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1917 NNRAFREQEIRMQEHRMAEHRLTQQHQRERERERDIVHLREKEEHRLHREKELQQQLEHRLAVQQHHQHREK--DFQQQ- 1993
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElaELPERl 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1994 ---EHRLAPQREKDIHVEHARLQIREKDipHEHRLIHQQREKEIHQQIAAQREKEHEHRLAVQQREKEIQHQEQRLAIQQ 2070
Cdd:COG4717 149 eelEERLEELRELEEELEELEAELAELQ--EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180
....*....|....*....|....
gi 1418074753 2071 QRENPHVVGSPIQQHAERLAAQQR 2094
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARL 250
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1909-2096 |
2.71e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1909 RLLADRYDNnrafREQEIRMQEHRMAEHRLTQQHQRERERERDivhlREKEEHRLHREkELQQQLEHRLAVQQHHQHREK 1988
Cdd:COG1196 228 ELLLLKLRE----LEAELEELEAELEELEAELEELEAELAELE----AELEELRLELE-ELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1989 DFQQQEHRLApQREKDIHVEHARLQIREKDIphEHRLIHQQREKEIHQQIAAQREKEHEHRLAVQQREKEIQHQEQRLAI 2068
Cdd:COG1196 299 RLEQDIARLE-ERRRELEERLEELEEELAEL--EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180
....*....|....*....|....*...
gi 1418074753 2069 QQQREnphvvgspIQQHAERLAAQQRER 2096
Cdd:COG1196 376 EAEEE--------LEELAEELLEALRAA 395
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1909-2096 |
3.15e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 58.01 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1909 RLLADRYDNNRAFREQEIRMQEhrmaEHRLTQQHQRERERE---RDIVHLREKEEhrlhREKELQQQLEHRLAVQQhhQH 1985
Cdd:pfam13868 116 AEAEEKLEKQRQLREEIDEFNE----EQAEWKELEKEEEREedeRILEYLKEKAE----REEEREAEREEIEEEKE--RE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1986 REKDFQQQEHRLAPQREKDIHveHARLQIREKDIPHEHRLIHQQREK-EIHQQIAAQREKEHEHRLAVQQREKEIQHQEQ 2064
Cdd:pfam13868 186 IARLRAQQEKAQDEKAERDEL--RAKLYQEEQERKERQKEREEAEKKaRQRQELQQAREEQIELKERRLAEEAEREEEEF 263
|
170 180 190
....*....|....*....|....*....|..
gi 1418074753 2065 RLAIQQQREnphvvgspiQQHAERLAAQQRER 2096
Cdd:pfam13868 264 ERMLRKQAE---------DEEIEQEEAEKRRM 286
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
407-628 |
3.72e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 407 NTQEDALRSTKDELLQQIGKVDREIAKRENQLNMLRKRIKELEEAANKpleatgLKRNIEEQSQQPKHQslaQKIYAENR 486
Cdd:COG4942 40 EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE------LEKEIAELRAELEAQ---KEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 487 RKAEEAHRLmeklgPKIELPLYNQPSDTSVYQENRTRHQTCMRTRLIARLRRDHTERASLHQQQTQTYTILVQewhrKVE 566
Cdd:COG4942 111 RALYRLGRQ-----PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA----LLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1418074753 567 RLEATQKRKSKETKNReffEKVFPELRKQREDKERfnRVGARIKSEADLEEIMDGLQEQEEE 628
Cdd:COG4942 182 ELEEERAALEALKAER---QKLLARLEKELAELAA--ELAELQQEAEELEALIARLEAEAAA 238
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1922-2097 |
4.17e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1922 REQEIRMQEHRMAEHRLTQQHQRERERERDivhLREKEEHRLHREKELQQQLEHRLAVQQHHQHREKDFQQQEHRLApQR 2001
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAE---LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA-RL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 2002 EKDIHVEHARLQIREKDIpheHRLihQQREKEIHQQIAAQREKEHEHRLAVQQREKEIQHQEQRLAIQQQREnphvvgsp 2081
Cdd:COG1196 301 EQDIARLEERRRELEERL---EEL--EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL-------- 367
|
170
....*....|....*.
gi 1418074753 2082 IQQHAERLAAQQRERD 2097
Cdd:COG1196 368 LEAEAELAEAEEELEE 383
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1911-2097 |
1.14e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.44 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1911 LADRYDNNRAFREQEIRMQEHRMAE-HRLTQQHQR------------------ERERERDIV-HLREKEEHRLHREKELQ 1970
Cdd:pfam17380 355 QEERKRELERIRQEEIAMEISRMRElERLQMERQQknervrqeleaarkvkilEEERQRKIQqQKVEMEQIRAEQEEARQ 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1971 QQLEH------------RLAVQQHHQHREKDFQQQEHR------LAPQREKDIHVEHARLQIREKDIPHEHR-LIHQQRE 2031
Cdd:pfam17380 435 REVRRleeeraremervRLEEQERQQQVERLRQQEEERkrkkleLEKEKRDRKRAEEQRRKILEKELEERKQaMIEEERK 514
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 2032 KEIHQQIAAQREK----EHEHRLAVQQREKEIQHQEQRLAIQQQREnphvvgspIQQHAERLAAQQRERD 2097
Cdd:pfam17380 515 RKLLEKEMEERQKaiyeEERRREAEEERRKQQEMEERRRIQEQMRK--------ATEERSRLEAMERERE 576
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1923-2097 |
1.50e-07 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 56.20 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1923 EQEIRMQEH-----RMAEHRLTQQHQRERERERDIVHLREKEEHRLHREKELQQQLEHRLAVQQHHQHREKDFQQQEHRL 1997
Cdd:pfam15558 102 DQENQRQEKlerarQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQ 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1998 APQREKDiHVEHARLQIREKDIphEHRL-----IHQQREKEIHQQIAAQREKEHEHRLAVQQR--EKEIQHQE-----QR 2065
Cdd:pfam15558 182 ARKVLVD-CQAKAEELLRRLSL--EQSLqrsqeNYEQLVEERHRELREKAQKEEEQFQRAKWRaeEKEEERQEhkealAE 258
|
170 180 190
....*....|....*....|....*....|....*
gi 1418074753 2066 LA---IQQQRENPHVVgspIQQHAERLAAQQRERD 2097
Cdd:pfam15558 259 LAdrkIQQARQVAHKT---VQDKAQRARELNLERE 290
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1920-2097 |
1.57e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1920 AFREQEIRMQEHRMAEHRLTQQHQRErerERDIVHLREKEEHRLHR----EKELQQQLEHRLAVQQHHQHREKDFQQQEH 1995
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARL---EQDIARLEERRRELEERleelEEELAELEEELEELEEELEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1996 RLAPQREKDIHVEHARLQIREKdiphehRLIHQQREKEIHQQIAAQREKEHEHRLAVQQREKEIQHQEQRLAIQQQREnp 2075
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAE------LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL-- 423
|
170 180
....*....|....*....|..
gi 1418074753 2076 hvvgspiQQHAERLAAQQRERD 2097
Cdd:COG1196 424 -------EELEEALAELEEEEE 438
|
|
| Myb_DNA-bind_6 |
pfam13921 |
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ... |
1159-1197 |
1.81e-07 |
|
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.
Pssm-ID: 372817 [Multi-domain] Cd Length: 60 Bit Score: 50.00 E-value: 1.81e-07
10 20 30
....*....|....*....|....*....|....*....
gi 1418074753 1159 WTDEELEQLRKALREYGTNWPKIAEQIPGKTSQQCKNYY 1197
Cdd:pfam13921 1 WTEEEDEKLLKLVEKYGNDWKQIAKELGRRTPKQCFDRW 39
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1914-2092 |
2.06e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 56.26 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1914 RYDNNRAFREQEIRMQEHRMAEHRLTQQHQRERERERDIvhlREKEEHRLHREKELQQQLEHRLAVQQHHQ-HREKDFQQ 1992
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRE---RNQQRQEARREREELQREEERLVQKEEQLdARAEKLDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1993 QEHRLApQREKDIHVEHARLQIREKDIPHEHRLIHQQREKEIHQQIAAQREKEHEHRLAVqqrekEIQHQEQRLAIQQQR 2072
Cdd:PRK12705 103 LENQLE-EREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQ-----RVKKIEEEADLEAER 176
|
170 180
....*....|....*....|
gi 1418074753 2073 ENPHVVGSPIQQHAERLAAQ 2092
Cdd:PRK12705 177 KAQNILAQAMQRIASETASD 196
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1922-2073 |
3.61e-07 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 55.04 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1922 REQEIRMQEHRMAEHrLTQQHQRERERERDIVHLREKEEHRLHREKELQQQLEHRLAVQQHHQHREKDFQQQEHRLAPQR 2001
Cdd:pfam15558 17 HKEEQRMRELQQQAA-LAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESR 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1418074753 2002 EKDIH--VEHARLQIREKDIPH-EHRLIHQ-QREKEIHQQIAAQREKEHehrLAVQQREKEIQHQEQRLAIQQQRE 2073
Cdd:pfam15558 96 WREQAedQENQRQEKLERARQEaEQRKQCQeQRLKEKEEELQALREQNS---LQLQERLEEACHKRQLKEREEQKK 168
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1922-2097 |
1.50e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.00 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1922 REQEIRMQEHRMAEHRLTQQHQRERERER--DIVHLREK-----EEHRLHREKELQQQLEHRLAVQQH-HQHREKDFQQ- 1992
Cdd:pfam13868 39 KEEERRLDEMMEEERERALEEEEEKEEERkeERKRYRQEleeqiEEREQKRQEEYEEKLQEREQMDEIvERIQEEDQAEa 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1993 ------------------QEHRLAPQREK------DIHVEHARLQIREKDIPHEHRLIHQQREKE-IHQQIAAQREKEHE 2047
Cdd:pfam13868 119 eeklekqrqlreeidefnEEQAEWKELEKeeereeDERILEYLKEKAEREEEREAEREEIEEEKErEIARLRAQQEKAQD 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1418074753 2048 HR--------------LAVQQREKEIQ----HQEQRLAIQQQREnphvvgspiQQHAERLAAQQRERD 2097
Cdd:pfam13868 199 EKaerdelraklyqeeQERKERQKEREeaekKARQRQELQQARE---------EQIELKERRLAEEAE 257
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1908-2060 |
1.50e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.00 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1908 DRLLADRY--DNNRAFREQEIRMQEHRMAEHRLTQQHQRERERERDIVHLREKEEHRLHREKELQQQLEHRLAVQQHHQH 1985
Cdd:pfam13868 204 DELRAKLYqeEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEK 283
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1418074753 1986 REKdfQQQEHRLAPQRekdihveharlQIREKdipheHRLIHQQREKEIHQQIAAQREKEHEHRLAVQQREKEIQ 2060
Cdd:pfam13868 284 RRM--KRLEHRRELEK-----------QIEER-----EEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
412-646 |
1.72e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 412 ALRSTKDELLQQIGKVDREIAKRENQLNMLRKRIKELE---EAANKPLEATG------LKRNIEEQSQQpkhQSLAQKIY 482
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEqllEELNKKIKDLGeeeqlrVKEKIGELEAE---IASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 483 AENRRKAEEAHRLMEKLGPKIE-LPLYNQPSDTSVYQENRTRHQtcmrtrLIARLRRDHTERASLH---QQQTQTYTILV 558
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDkLLAEIEELEREIEEERKRRDK------LTEEYAELKEELEDLRaelEEVDKEFAETR 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 559 QEWHRKVERLEATQKRKSKETKNReffEKVFPELRKQREDKERFNRVGARIKS-----EADLEEIMDGLQEQEE--ETLQ 631
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKREL---DRLQEELQRLSEELADLNAAIAGIEAkinelEEEKEDKALEIKKQEWklEQLA 461
|
250
....*....|....*
gi 1418074753 632 DLKNSIKAcQLEDKK 646
Cdd:TIGR02169 462 ADLSKYEQ-ELYDLK 475
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1383-1689 |
2.66e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.40 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1383 PPTTAHSPPSTTSNSNPLTVKDLMLGVIEMQLKRTPNSPADGGGSSAPNSSGTPTISSILKTDHRNDI----------TY 1452
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPpaapaagpprRL 2783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1453 VRGYKSSSNMTNTALPSRDTNLATLSVVSGPHHGHRSAPSPQQISQMQATITPCPPAAPSnqGSSSDLLPKEGLVVMQVQ 1532
Cdd:PHA03247 2784 TRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP--GPPPPSLPLGGSVAPGGD 2861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1533 QALRETEGTLDLSIKKPRlqqdynhsiqlhKPPTVTLYRPEPPPGAYYHPHTTPHPEQGRNAKSPLVYASAPRPQASITP 1612
Cdd:PHA03247 2862 VRRRPPSRSPAAKPAAPA------------RPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQP 2929
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1418074753 1613 KMNKVTVPQTHPKLSPKLGSMSTPGHKGGSITHGTPVSTARYEGLLRQMTPPGNPPVSGASANVSERGGGAVNASSA 1689
Cdd:PHA03247 2930 QPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSS 3006
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
394-791 |
3.16e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.05 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 394 PQTEAISPTLPEPNTqedalrSTKDELLQQIGKVDREIAKRENQLNMLRKRIKELEE---AANKPLEATGLKRN----IE 466
Cdd:TIGR00618 513 PNPARQDIDNPGPLT------RRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEqmqEIQQSFSILTQCDNrskeDI 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 467 EQSQQPKH--QSLAQKIYAENRRKAEEAHRLMEKLGPKI---ELPLYNQPSDTSVYQENRTRHQTcmrtrLIARLRRDHT 541
Cdd:TIGR00618 587 PNLQNITVrlQDLTEKLSEAEDMLACEQHALLRKLQPEQdlqDVRLHLQQCSQELALKLTALHAL-----QLTLTQERVR 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 542 ERASLHQQQTQTYtilvqeWHRKVERLEATQKRKSKETKNREFFEKVFPELRKQRE-----DKERFNRVGARIKSEADLE 616
Cdd:TIGR00618 662 EHALSIRVLPKEL------LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELEThieeyDREFNEIENASSSLGSDLA 735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 617 EIMDGLQEQEEETLQDLKNSIKAcQLEDKKMRSYAVIPPLLLDAKQRRIAfqnRNGLLQPEELEALHSERKLInvwssve 696
Cdd:TIGR00618 736 AREDALNQSLKELMHQARTVLKA-RTEAHFNNNEEVTAALQTGAELSHLA---AEIQFFNRLREEDTHLLKTL------- 804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 697 hesfKEKYLQHPKNYGVIAQSLEHKGVQDcvhhyyltkkTENYKQLLRKSrqrtrssrnnpnnkvnntSSTIGSIDILTT 776
Cdd:TIGR00618 805 ----EAEIGQEIPSDEDILNLQCETLVQE----------EEQFLSRLEEK------------------SATLGEITHQLL 852
|
410
....*....|....*
gi 1418074753 777 GVTTRLQREQQKTQE 791
Cdd:TIGR00618 853 KYEECSKQLAQLTQE 867
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1906-2095 |
3.83e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1906 MADRLlaDRYDNNRAFREQEIRMQEHRMAEHR--LTQQHQRERERERDIVHLREKEEHRLHREKELQQQL----EHRLAV 1979
Cdd:TIGR02169 679 LRERL--EGLKRELSSLQSELRRIENRLDELSqeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLssleQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1980 QQHHQHREKDFQQQEHRLAPQREK--DIHVEHARLQIREKDipHEHRLIHQQReKEIHQQIAAQREKEHEHRLAVQQREK 2057
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEAlnDLEARLSHSRIPEIQ--AELSKLEEEV-SRIEARLREIEQKLNRLTLEKEYLEK 833
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1418074753 2058 EIQH--------QEQRLAIQQQRENPHVVGSPIQQHAERLAAQQRE 2095
Cdd:TIGR02169 834 EIQElqeqridlKEQIKSIEKEIENLNGKKEELEEELEELEAALRD 879
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
408-792 |
4.29e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.28 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 408 TQEDALRSTKDELLQQIGKVDREIAKRENQLNMLRKRIKELEEAANKPLEATGLKRNIE-EQSQQPKHQSLAQKIyaenR 486
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQiEQQAQRIHTELQSKM----R 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 487 RKAEEAHRLMEKLGPKIELPLYNQPSDTSVYQENRTRHQTCMRTRLIARLRRDHTERASLHQQQTQTYTILvqewhrkvE 566
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLT--------Q 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 567 RLEATQKRKSKEtknREFFEKVFPELRKQREDKERFnrvgARIKSEADLEEIMDGLQEQE-EETLQDLKNSIKACQledk 645
Cdd:TIGR00618 394 KLQSLCKELDIL---QREQATIDTRTSAFRDLQGQL----AHAKKQQELQQRYAELCAAAiTCTAQCEKLEKIHLQ---- 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 646 KMRSYavippllLDAKQRRIAfQNRNGLLQPEELEALHSERKLinvwSSVEHESFKEKYLQHPKNYGVIA------QSLE 719
Cdd:TIGR00618 463 ESAQS-------LKEREQQLQ-TKEQIHLQETRKKAVVLARLL----ELQEEPCPLCGSCIHPNPARQDIdnpgplTRRM 530
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1418074753 720 HKGVQDCVHHYYLTKKTENYKQLLRKSRQRTRSSRNNPNNKVNNTSSTIGSIDILTTGVTTRLQREQQKTQEN 792
Cdd:TIGR00618 531 QRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL 603
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1922-2064 |
4.46e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.88 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1922 REQEIRMQEHRMAEHRLTQQHQRERERERDiVHLREKEEhrlhREKELQQQLEHRLAVQQHHQHRekdfQQQEHRLA--- 1998
Cdd:pfam15709 380 LEQQRRFEEIRLRKQRLEEERQRQEEEERK-QRLQLQAA----QERARQQQEEFRRKLQELQRKK----QQEEAERAeae 450
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1418074753 1999 PQREKDIHVEHARLQIREKDIPHEHRLIHQ---QREKEIHQQIAAQREKEHEHRLAVQQREKEIQHQEQ 2064
Cdd:pfam15709 451 KQRQKELEMQLAEEQKRLMEMAEEERLEYQrqkQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQ 519
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1935-2093 |
5.66e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.89 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1935 EHRLTQQHQRERERERDIVHLREKEEHRLHREKELQQQL----EHRLAVQQHHQHREK-DFQQQEHRLAPQREKDIHVE- 2008
Cdd:TIGR00618 228 LKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRarieELRAQEAVLEETQERiNRARKAAPLAAHIKAVTQIEq 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 2009 -----HARLQIREKDIPHE--HRLIHQQREKEIHQQ-----------------------IAAQREKEHE--HRLAVQQRE 2056
Cdd:TIGR00618 308 qaqriHTELQSKMRSRAKLlmKRAAHVKQQSSIEEQrrllqtlhsqeihirdahevatsIREISCQQHTltQHIHTLQQQ 387
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1418074753 2057 KEIQHQEQRLA---------IQQQRENPHVVGSPIQQHAERLAAQQ 2093
Cdd:TIGR00618 388 KTTLTQKLQSLckeldilqrEQATIDTRTSAFRDLQGQLAHAKKQQ 433
|
|
| Activator_LAG-3 |
pfam11498 |
Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of ... |
1775-2048 |
5.99e-06 |
|
Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of growth, differentiation and patterning in animal development, relies on either of the receptors GLP-1 or LIN-12. Both these receptors promote signalling by the recruitment of LAG-3 to target promoters, where it then acts as a transcriptional activator. LAG-3 works as a ternary complex together with the DNA binding protein, LAG-1. Its N-terminal region adopts an elongated kinked helix that is required for complex assembly.
Pssm-ID: 151935 [Multi-domain] Cd Length: 476 Bit Score: 51.50 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1775 PSYTMEQQLSSRQ---IIM----NDYITSQQMHARARGSGSTGA--SVTGEMASKNEPPPSNLYYASTPPPPPPQTHTQP 1845
Cdd:pfam11498 157 PQFQMQQQYHSQQqqyIMMaaqhHHFMGMQQIHHQMPSTSSADAihSVPTPAGSIHQPSPAEMQNGCGMSRNATMDMTCS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1846 RQGVIQRHNPQKQMHYPPPPILDAFSNLVEVAIKQPTLPVPHQHGHPPSGSGGHEGLGKTMADRLLADRYDNNR-----A 1920
Cdd:pfam11498 237 PMSGGLPISDENNLAVPEGEWFDKLALAVAEKYDADTILGPDTYDTFLAELDAMEPEGETKKSPMEAGGDRMPQsapppA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1921 FREQEIRMQEHRMAEHRLTQQHQR-----ERERERDIVHLREKEEHRLHREKEL---QQQLEHRLavQQHHQ-HREKDFQ 1991
Cdd:pfam11498 317 MNPQHIAQLAQQQNKMRLLQQQEMemqriEQQRQQQIMHQHQQQQQQEHQQQQMllqQQQQMHQL--QQHHQmNGGGQFA 394
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1418074753 1992 QQEHRLAPQREKdihVEHARLQIREKdiphehrliHQQREKEIHQQIAAQREKEHEH 2048
Cdd:pfam11498 395 TQAHQHAAYLQQ---MQHMRLQEQIQ---------HQQQQAQHHQQAQQQHQQPAQH 439
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1940-2096 |
6.07e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.41 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1940 QQHQRERERERDiVHLREKEEHRLHREKELQQQLE---HRLAVQQhhqhREKDFQQQEHRLAPQREKdihveharlqire 2016
Cdd:COG2268 200 DARIAEAEAERE-TEIAIAQANREAEEAELEQEREietARIAEAE----AELAKKKAEERREAETAR------------- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 2017 kdiphehrlIHQQREKEIhQQIAAQREKEHEHRLAVQQREKEIQHQEQRLAIQQQRENphvVGSPIQqhAERLAAQQRER 2096
Cdd:COG2268 262 ---------AEAEAAYEI-AEANAEREVQRQLEIAEREREIELQEKEAEREEAELEAD---VRKPAE--AEKQAAEAEAE 326
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1921-2096 |
7.16e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.66 E-value: 7.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1921 FREQEIRMQEHRMAEHRLTQQHQRER-ERERdivhLREKEEHRLhREKELQQQLEHRLAVQQHHQHREKDFQQQEHRLAP 1999
Cdd:pfam17380 270 FLNQLLHIVQHQKAVSERQQQEKFEKmEQER----LRQEKEEKA-REVERRRKLEEAEKARQAEMDRQAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 2000 QREKDIhvEHARL--------QIREKDIPHEH---------RLIHQQREKEIHQQIAAQR-----EKEHEHRLAVQQREK 2057
Cdd:pfam17380 345 EREREL--ERIRQeerkreleRIRQEEIAMEIsrmrelerlQMERQQKNERVRQELEAARkvkilEEERQRKIQQQKVEM 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1418074753 2058 EI---------QHQEQRLAIQQQRENPHVVGSPI--QQHAERLAAQQRER 2096
Cdd:pfam17380 423 EQiraeqeearQREVRRLEEERAREMERVRLEEQerQQQVERLRQQEEER 472
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1927-2095 |
7.44e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 7.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1927 RMQEHRMAEHRLTQQHQRERERERDIVHLREK-EEH-RLHREKELQQQLEHRLAVQqhhqhrekdFQQQEHRLAPQREKD 2004
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAREQIELLEPIRELaERYaAARERLAELEYLRAALRLW---------FAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 2005 IHVEHARLQIREKDIPHEHRLIHQQREkEIHQQIAA---QREKEHEHRLAvqQREKEIQHQEQRLAIQQQREnpHVVGSP 2081
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELD-ELEAQIRGnggDRLEQLEREIE--RLERELEERERRRARLEALL--AALGLP 374
|
170
....*....|....
gi 1418074753 2082 IQQHAERLAAQQRE 2095
Cdd:COG4913 375 LPASAEEFAALRAE 388
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1938-2073 |
1.67e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1938 LTQQHQRERERERDIvhlrEKEEHRLHREKE-LQQQLEHRLAVQQHHQHREKDFQQQEHRLAPQREKdIHVEHARLQIRE 2016
Cdd:TIGR02169 803 LEEEVSRIEARLREI----EQKLNRLTLEKEyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE-LEEELEELEAAL 877
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1418074753 2017 KDIphEHRLIHQQREKEIHQ-QIAAQREKEHEHRLAVQQREKEIQHQEQRLAIQQQRE 2073
Cdd:TIGR02169 878 RDL--ESRLGDLKKERDELEaQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
418-686 |
1.80e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 418 DELLQQIGKVDREIAKRENQLNMLRKRIKELEEaankplEATGLKRNIEEQSQQ------------PKHQSLAQKI---- 481
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEE------ELEQLRKELEELSRQisalrkdlarleAEVEQLEERIaqls 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 482 --YAENRRKAEEAHRLMEKLGPKIELPLYNQPSDTSVYQENRTRHQTcmRTRLIARLRRDHTERASLHQQQTQTYTILVQ 559
Cdd:TIGR02168 754 keLTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA--LREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 560 EWHRKVERLEATQKRKSKETKNREFFEKVFPELRKQRED---------KERFNRVGARIKSEADLEEIMDGLQEQEEEtL 630
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEleseleallNERASLEEALALLRSELEELSEELRELESK-R 910
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1418074753 631 QDLKNSIKACQ--LEDKKMRsyavipplLLDAKQRRIAFQNR---NGLLQPEELEALHSER 686
Cdd:TIGR02168 911 SELRRELEELRekLAQLELR--------LEGLEVRIDNLQERlseEYSLTLEEAEALENKI 963
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
407-641 |
1.81e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 407 NTQEDALRSTKDELLQQIGKVDREIAKRENQLNMLRKRIKELEEAAN---KPLEATG-----LKRNIEEQSQQPKH---- 474
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEelqKELYALAneisrLEQQKQILRERLANlerq 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 475 QSLAQKIYAENRRKAEEAHRLMEKLGPKIElPLYNQPSDTSVYQENRTRHQTCMRTRLIArLRRDHTERAS-----LHQQ 549
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLE-ELKEELESLEAELEELEAELEELESRLEE-LEEQLETLRSkvaqlELQI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 550 QTQTYTILVQEwhRKVERLEATQKRKSKETK--NREFFEKVFPELRKQ--REDKERFNRVGARIKSEADLEEIMDGLQEQ 625
Cdd:TIGR02168 396 ASLNNEIERLE--ARLERLEDRRERLQQEIEelLKKLEEAELKELQAEleELEEELEELQEELERLEEALEELREELEEA 473
|
250
....*....|....*.
gi 1418074753 626 EEEtLQDLKNSIKACQ 641
Cdd:TIGR02168 474 EQA-LDAAERELAQLQ 488
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
412-705 |
2.76e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 412 ALRSTKDELLQQIGKVDREIAKRENQLNMLRKRIKELEEAANKPLEATGLKRNIEEQSQ--QPKHqslaqKIYAENRRKA 489
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEelEERH-----ELYEEAKAKK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 490 EEAHRLMEKLGP----KIElplynqpsdtSVYQENRTRHQTCMRTR--LIARLRRDHTERASL----------------- 546
Cdd:PRK03918 372 EELERLKKRLTGltpeKLE----------KELEELEKAKEEIEEEIskITARIGELKKEIKELkkaieelkkakgkcpvc 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 547 -------HQQQtqtytiLVQEWHRKVERLEATQKR-KSKETKNREFFEKV------FPELRKQREDKERFNRVGARIKsE 612
Cdd:PRK03918 442 grelteeHRKE------LLEEYTAELKRIEKELKEiEEKERKLRKELRELekvlkkESELIKLKELAEQLKELEEKLK-K 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 613 ADLEEIMDGLQEQEE--ETLQDLKNSIKACQLEDKKMRSYavippllldaKQRRIAFQNRNGLLQpEELEALHseRKLIN 690
Cdd:PRK03918 515 YNLEELEKKAEEYEKlkEKLIKLKGEIKSLKKELEKLEEL----------KKKLAELEKKLDELE-EELAELL--KELEE 581
|
330 340
....*....|....*....|....
gi 1418074753 691 V-WSSVEH--------ESFKEKYL 705
Cdd:PRK03918 582 LgFESVEEleerlkelEPFYNEYL 605
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1904-2092 |
2.98e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.18 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1904 KTMADRLLADRYDNNRAFREQEIRMQEhrmaEHRLTQQHQRERER----ERDIVHLREKEEHRLHR----EKELQQQLEH 1975
Cdd:pfam15709 332 KASRDRLRAERAEMRRLEVERKRREQE----EQRRLQQEQLERAEkmreELELEQQRRFEEIRLRKqrleEERQRQEEEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1976 RLAVQQHHQHREKDFQQQE--HRLAPQREKDIHVEHARLQIREKdiphehrlihqQREKEIHQQIAAQR----EKEHEHR 2049
Cdd:pfam15709 408 RKQRLQLQAAQERARQQQEefRRKLQELQRKKQQEEAERAEAEK-----------QRQKELEMQLAEEQkrlmEMAEEER 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1418074753 2050 LAVQQREKEIQHQEQRLA---IQQQRENPHVVGSPIQQHAERLAAQ 2092
Cdd:pfam15709 477 LEYQRQKQEAEEKARLEAeerRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
410-621 |
3.65e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 410 EDALRSTKDELLQQIGKVDREIAKRENQL--------NMLRKRIKELEEAANKPLEATGLKRNIEEQsqQPKHQSLAQKI 481
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKELeelgfesvEELEERLKELEPFYNEYLELKDAEKELERE--EKELKKLEEEL 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 482 yAENRRKAEEAHRLMEKLGPKIE--LPLYNQPSdtsvYQENRTRHqtcmrTRLIARLRRDHTERASLHQQqtqtytilVQ 559
Cdd:PRK03918 629 -DKAFEELAETEKRLEELRKELEelEKKYSEEE----YEELREEY-----LELSRELAGLRAELEELEKR--------RE 690
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1418074753 560 EWHRKVERLEATQKRKSKETKNREFFEKVFPELRKQRED--------KER-FNRVGaRIKSEAdLEEIMDG 621
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKvkkykallKERaLSKVG-EIASEI-FEELTEG 759
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
410-635 |
3.84e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 410 EDALRSTKDEL---LQQIGKVDREIAKRENQLNMLRKRIKELEEAANkplEATGLKRNIEEQSQQPKhqSLAQKIyAENR 486
Cdd:PRK03918 192 EELIKEKEKELeevLREINEISSELPELREELEKLEKEVKELEELKE---EIEELEKELESLEGSKR--KLEEKI-RELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 487 RKAEEAHRLMEKLGPKI-ELPLYNQPSDTsvYQE-NRTRHQTCMRTRLIARLRRDHTERASLHQQQtqtytilVQEWHRK 564
Cdd:PRK03918 266 ERIEELKKEIEELEEKVkELKELKEKAEE--YIKlSEFYEEYLDELREIEKRLSRLEEEINGIEER-------IKELEEK 336
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1418074753 565 VERLEATQKRKsKETKNR-EFFEKVFPELRKQREDKERFNRVGARIKSEA--DLEEIMDGLQEQEEETLQDLKN 635
Cdd:PRK03918 337 EERLEELKKKL-KELEKRlEELEERHELYEEAKAKKEELERLKKRLTGLTpeKLEKELEELEKAKEEIEEEISK 409
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1922-2097 |
4.15e-05 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 48.52 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1922 REQEI---RMQEHRMAEHRLTQQHQRERERerdivhLREKEEHRLhrekELQQQLEHRlavqqhHQHREKDFQQQEHRLA 1998
Cdd:pfam15742 93 RELELevlKQAQSIKSQNSLQEKLAQEKSR------VADAEEKIL----ELQQKLEHA------HKVCLTDTCILEKKQL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1999 PQREKDIHVEHARL--QIREKdipHEHRLIHQQREKEIHQQIAAQREKEHEHRLAVQQREKEIQHQEQRLAIQQ---QRE 2073
Cdd:pfam15742 157 EERIKEASENEAKLkqQYQEE---QQKRKLLDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLEnekRKS 233
|
170 180
....*....|....*....|....
gi 1418074753 2074 NPHVVGSpiQQHAERLAAQQRERD 2097
Cdd:pfam15742 234 DEHLKSN--QELSEKLSSLQQEKE 255
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1427-1885 |
5.72e-05 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 48.76 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1427 SSAPNSSGT-PTISSIlktdhrndityvrGYKSSSnmTNTALPSRD---TNLaTLSVVSGP--HHGHRSAPSPQQISQMQ 1500
Cdd:pfam05109 422 SKAPESTTTsPTLNTT-------------GFAAPN--TTTGLPSSThvpTNL-TAPASTGPtvSTADVTSPTPAGTTSGA 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1501 ATITPCPpaAPSNQGSSS---DLLPKEGLVVMQVQQAlreTEGTLDLSIKKPrlqqdynhsiqlhKPPTVTLYRPEPPPG 1577
Cdd:pfam05109 486 SPVTPSP--SPRDNGTESkapDMTSPTSAVTTPTPNA---TSPTPAVTTPTP-------------NATSPTLGKTSPTSA 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1578 AyyhphTTPHPeqgrNAKSPLVYASAPRPQASI-----TPKMNKVTVPqTHPKLSPKLGSMS----TPGHKGGSiTHGTP 1648
Cdd:pfam05109 548 V-----TTPTP----NATSPTPAVTTPTPNATIptlgkTSPTSAVTTP-TPNATSPTVGETSpqanTTNHTLGG-TSSTP 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1649 VSTARYEGLLRQMTPPGNPPVSGASANVSERGGG---------AVNASSAGP--GAPKETGGGSITQGTPVLPfavdkrg 1717
Cdd:pfam05109 617 VVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSisetlspstSDNSTSHMPllTSAHPTGGENITQVTPAST------- 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1718 apiyDYHRTIRHSPVTGSGNVPPPPGQGPPSQATSPAVVVSHGGSqynsysaagrpPPSYTMEQQLSSRQIIMNDYITSQ 1797
Cdd:pfam05109 690 ----STHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGT-----------PPKNATSPQAPSGQKTAVPTVTST 754
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1798 QMHArarGSGSTGASVTGEMASKNEPP----------PSNLYYASTPPPPPPQTHTQPRQGVIQRHNPQKQMHYPPPPIL 1867
Cdd:pfam05109 755 GGKA---NSTTGGKHTTGHGARTSTEPttdyggdsttPRTRYNATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPTS 831
|
490
....*....|....*....
gi 1418074753 1868 DA-FSNLVEVAIKQPTLPV 1885
Cdd:pfam05109 832 QPrFSNLSMLVLQWASLAV 850
|
|
| SANT_TRF |
cd11660 |
Telomere repeat binding factor-like DNA-binding domains of the SANT/myb-like family; Human ... |
1157-1195 |
6.90e-05 |
|
Telomere repeat binding factor-like DNA-binding domains of the SANT/myb-like family; Human telomere repeat binding factors, TRF1 and TRF2, function as part of the 6 component shelterin complex. TRF2 binds DNA and recruits RAP1 (via binding to the RAP1 protein c-terminal (RCT)) and TIN2 in the protection of telomeres from DNA repair machinery. Metazoan shelterin consists of 3 DNA binding proteins (TRF2, TRF1, and POT1) and 3 recruited proteins that bind to one or more of these DNA-binding proteins (RAP1, TIN2, TPP1). Schizosaccharomyces pombe TAZ1 is an orthlog and binds RAP1. Human TRF1 and TRF2 bind double-stranded DNA. hTRF2 consists of a basic N-terminus, a TRF homology domain, the RAP1 binding motif (RBM), the TIN2 binding motif (TBM) and a myb-like DNA binding domain, SANT, named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. Tandem copies of the domain bind telomeric DNA tandem repeats as part of the capping complex. The single myb-like domain of TRF-type proteins is similar to the tandem myb_like domains found in yeast RAP1.
Pssm-ID: 212558 [Multi-domain] Cd Length: 50 Bit Score: 42.17 E-value: 6.90e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1418074753 1157 RPWTDEELEQLRKALREYGT-NWPKIAEQ---IPGKTSQQCKN 1195
Cdd:cd11660 1 RKWTDEEDEALVEGVEKYGVgNWAKILKDyffVNNRTSVDLKD 43
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1907-2094 |
7.78e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1907 ADRLLADRYDNNRAFREQEIRMQEHRMAEHRLTQQHQR-ERERERDIVHLREKEEhRLHREKELQQQLEHRLA------- 1978
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESlERRIAATERRLEDLEE-QIEELSEDIESLAAEIEeleelie 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1979 -VQQHHQHREKDFQQQEHRLAPQREkdiHVEHARLQIREKDiphehrlihqQREKEIHQQIAAQREKEHEHRLAVQQREK 2057
Cdd:TIGR02168 870 eLESELEALLNERASLEEALALLRS---ELEELSEELRELE----------SKRSELRRELEELREKLAQLELRLEGLEV 936
|
170 180 190
....*....|....*....|....*....|....*..
gi 1418074753 2058 EIQHQEQRLAIQQQRENPHVVGSPIQQHAERLAAQQR 2094
Cdd:TIGR02168 937 RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1921-2065 |
8.66e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1921 FREQEIRMQEHRMAEHR--LTQQHQRERERERDIVHLREKEEhRLH---------REKELQQQLEHRlavQQHHQHREKD 1989
Cdd:COG4913 285 FAQRRLELLEAELEELRaeLARLEAELERLEARLDALREELD-ELEaqirgnggdRLEQLEREIERL---ERELEERERR 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1418074753 1990 FQQQEHRLAPQREKDIHVEHARLQIREKdiPHEHRLIHQQREKEIHQQIAAQREKEHEHRLAVQQREKEIQHQEQR 2065
Cdd:COG4913 361 RARLEALLAALGLPLPASAEEFAALRAE--AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1947-2095 |
9.21e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1947 ERERDIVHLREKEEHRLHREKELQQQLEhrlAVQQHHQHREKDFQQQEhRLAPQREKDIHVEHARLQIREKDIP-HEHRL 2025
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALA---ELRKELEELEEELEQLR-KELEELSRQISALRKDLARLEAEVEqLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 2026 IHQQRE-KEIHQQIAAQREKEHEHRLAVQQREKEIQHQEQRLA-------------------IQQQRENPHVVGSPIQQH 2085
Cdd:TIGR02168 750 AQLSKElTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEqlkeelkalrealdelraeLTLLNEEAANLRERLESL 829
|
170
....*....|
gi 1418074753 2086 AERLAAQQRE 2095
Cdd:TIGR02168 830 ERRIAATERR 839
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1900-2223 |
9.69e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.59 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1900 EGLGKTMADRLLADRYDNNRAFREQEIRMQEHRMAEHRLTQQHQRERERERDIVHLREKEEHRLHREKELQQQLEHRLAV 1979
Cdd:COG5278 144 SGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAA 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1980 QQHHQHREKdfQQQEHRLAPQREKDIHVEHARLQIREKDIPHEHRLIHQQREKEIHQQIAAQREKEHEHRLAVQQREKEI 2059
Cdd:COG5278 224 AALAALAAL--ELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 2060 QHQEQRLAIQQQRENPHVVGSPIQQHAERLAAQQRERDLLHLHQQHQQQQQQHMQHIQHQQRIEIERRHIAQLYRDQQQQ 2139
Cdd:COG5278 302 LELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 2140 QQQLDRDSSRLLSSGFSQSSRLQPSQQSQQQQQQSSSRQSQSSSQQQNDSSSTLTAASLIDAIITHQINQGVDNANASGS 2219
Cdd:COG5278 382 EGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAA 461
|
....
gi 1418074753 2220 STNQ 2223
Cdd:COG5278 462 EALA 465
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
1919-2041 |
1.08e-04 |
|
Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.
Pssm-ID: 399954 [Multi-domain] Cd Length: 148 Bit Score: 44.70 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1919 RAFREQEIR----MQEHRMAEHRLTQQHQ-RERERER--------------------DIVHLREKeehrlhrEKELQQQL 1973
Cdd:pfam07321 17 KAVKRQEQAlaaaRAAHQQAQASLQDYRAwRPQEEQRlyaeiqgklvllkelekvkqQVALLREN-------EADLEKQV 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1418074753 1974 EHrlAVQQHHQHREKDFQQQEHRLAPQREKDIHVEHARLQIREkdiphehRLIHQQREKEIHQQIAAQ 2041
Cdd:pfam07321 90 AE--ARQQLEAEREALRQARQALAEARRAVEKFAELVRLVQAE-------ELRQQERQEEQELEEFAE 148
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1911-2073 |
1.58e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1911 LADRYDNNRAFREQEIRMQEHRMAEHRLTQQHQRERERERDIVHLREKEEHRLHREKELQQQLEHRLAVQQHHQHREKDF 1990
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1991 QQQEHRLAPQREKDIHVEHARLQIRE--KDIPHEHRLIHQQREKEIHQQIAAQREKEHEHRLAVQQREKEIQHQEQRL-- 2066
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEeqLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgp 781
|
170
....*....|.
gi 1418074753 2067 ----AIQQQRE 2073
Cdd:COG1196 782 vnllAIEEYEE 792
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1933-2070 |
1.85e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 44.26 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1933 MAEHRLTQQHQRERE-RERdivhlREKEEHRLHREKELQQQLEhrlavQQHHQHREKDFQQQEHRlapQREKDihvEHAR 2011
Cdd:pfam05672 16 LAEKRRQAREQREREeQER-----LEKEEEERLRKEELRRRAE-----EERARREEEARRLEEER---RREEE---ERQR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1418074753 2012 LQIREKdiphehrliHQQREKEIHQQIAAQREKEHEHRLAvqQREKEIQHQEQRLAIQQ 2070
Cdd:pfam05672 80 KAEEEA---------EEREQREQEEQERLQKQKEEAEAKA--REEAERQRQEREKIMQQ 127
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
418-688 |
1.96e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 418 DELLQQIGKVDREIAKRENQLNMLRKRIKELEEAANKpleatgLKRNIEEQSQQpkHQSLAQKIYAENRRKAEEAHRLME 497
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEE------LRLELEELELE--LEEAQAEEYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 498 KLGPKIELplynqpsdtsvyQENRTRHQTcMRTRLIARLRRDHTERASLHQQQTQTYTIL----VQEWHRKVERLEATQK 573
Cdd:COG1196 307 LEERRREL------------EERLEELEE-ELAELEEELEELEEELEELEEELEEAEEELeeaeAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 574 RKSKETKNREFFEKVFPELRKQREDKERFNRVGARIKSEADLEEIMDGLQEQEEETLQDLKNSIKACQLEDKKMRSYAvi 653
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE-- 451
|
250 260 270
....*....|....*....|....*....|....*
gi 1418074753 654 ppLLLDAKQRRIAFQNRNGLLQPEELEALHSERKL 688
Cdd:COG1196 452 --AELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1943-2074 |
2.20e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 45.08 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1943 QRERERERdivhLREKEEHRLHREKELQQQlehRLAvQQHHQH--REKDFQQQEHRLAPQREKD-IHVEHARLQIREKDI 2019
Cdd:pfam13904 65 QRQRQKEL----QAQKEEREKEEQEAELRK---RLA-KEKYQEwlQRKARQQTKKREESHKQKAaESASKSLAKPERKVS 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1418074753 2020 PHEHRLIHQQREKEIHQQIAAQREKEHEHRLAvQQREKEIQHQEQRLAIQQQREN 2074
Cdd:pfam13904 137 QEEAKEVLQEWERKKLEQQQRKREEEQREQLK-KEEEEQERKQLAEKAWQKWMKN 190
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
1925-2044 |
2.90e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 45.33 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1925 EIRMQEHRMAEHRLTQQHQRERERERDIVH---LREKEEHRLHREKELQQQL-EHRLavQQHHQHREKDFQQQEHrlapq 2000
Cdd:pfam09728 116 QDKMEEKSEKNNKLREENEELREKLKSLIEqyeLRELHFEKLLKTKELEVQLaEAKL--QQATEEEEKKAQEKEV----- 188
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1418074753 2001 reKDIHVEHARLQirekdiphehrlIHQQREKEIHQQIAAQREK 2044
Cdd:pfam09728 189 --AKARELKAQVQ------------TLSETEKELREQLNLYVEK 218
|
|
| ClassIIa_HDAC4_Gln-rich-N |
cd10162 |
Glutamine-rich N-terminal helical domain of HDAC4, a Class IIa histone deacetylase; This ... |
1965-2050 |
3.01e-04 |
|
Glutamine-rich N-terminal helical domain of HDAC4, a Class IIa histone deacetylase; This family consists of the glutamine-rich domain of histone deacetylase 4 (HDAC4). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.
Pssm-ID: 197398 [Multi-domain] Cd Length: 90 Bit Score: 42.11 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1965 REKELQQQLehrLAVQQHHQHREK----DFQQQEHRLAPQREKDIHvEHARLQIREKDIPHEHRLIHQQREKEIHQQIAA 2040
Cdd:cd10162 5 REQQLQQEL---LALKQKQQIQRQlliaEFQRQHEQLSRQHEAQLH-EHIKQQQELLAMKHQQELLEHQRKLERHRQEQE 80
|
90
....*....|
gi 1418074753 2041 QREKEHEHRL 2050
Cdd:cd10162 81 MEKQQREQKL 90
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
408-648 |
3.36e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 408 TQEDALRSTKDELLQQIGKVDREIAKRENQLNMLRKRIKELeeaANKPLEATGLKRNIEEQSQqpKHQSLAQKIYAENRR 487
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKEL---AEKRDELNAQVKELREEAQ--ELREKRDELNEKVKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 488 KAEEAHRLMEKLgpkielplyNQPSDTsvYQENRTRHQTCMRTRL-IARLRR--DHTERaslhQQQTQTYTI-----LVQ 559
Cdd:COG1340 76 LKEERDELNEKL---------NELREE--LDELRKELAELNKAGGsIDKLRKeiERLEW----RQQTEVLSPeeekeLVE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 560 EWHRKVERLEATQKRKSKETKNREFFEKVfPELRKQRED--------KERFNRVGARI---KSEAD-LEEIMDGLQEQ-- 625
Cdd:COG1340 141 KIKELEKELEKAKKALEKNEKLKELRAEL-KELRKEAEEihkkikelAEEAQELHEEMielYKEADeLRKEADELHKEiv 219
|
250 260
....*....|....*....|....
gi 1418074753 626 -EEETLQDLKNSIKACQLEDKKMR 648
Cdd:COG1340 220 eAQEKADELHEEIIELQKELRELR 243
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
412-705 |
4.00e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 412 ALRstKDELLQQIgkvdrEIAKRENQLNMLRKRIKELEEAANKPLEATGLKRNIEEQSQQPKHQSLAQKIYAENRRKAEE 491
Cdd:PTZ00121 1579 ALR--KAEEAKKA-----EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE 1651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 492 AHRLMEKLGPKIELPLYNQPSDTSVYQENRTRHQTCMR-----------TRLIARLRRDHTE---RASLHQQQTQTYTIL 557
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKaaealkkeaeeAKKAEELKKKEAEekkKAEELKKAEEENKIK 1731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 558 VQEWHRKVERleatQKRKSKETKNREFFEKVFPELRKQREDKERFNRVGARIKSEADLEEIMDGLQEQEEETLQDLKNSI 637
Cdd:PTZ00121 1732 AEEAKKEAEE----DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNF 1807
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1418074753 638 KACQLEDKKMRSYAVIPPLLLDAKQRRIAFQNRNGLLQPEELEALHSERKLINVWSSVEHESF-KEKYL 705
Cdd:PTZ00121 1808 ANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFnKEKDL 1876
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1943-2094 |
5.44e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 45.33 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1943 QRERERE-RDIVHLREKEEHRLHREKELQQQLEHRlAVQQHHQHREKDFQQQEHRLAPQREKDIHVEHARLQIREKDIPH 2021
Cdd:pfam15709 327 KREQEKAsRDRLRAERAEMRRLEVERKRREQEEQR-RLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEE 405
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1418074753 2022 EHRliHQQREKEIHQQIAAQREKEHEHRLAVQQREKEiQHQEQRLAIQQQREnphvvgspiQQHAERLAAQQR 2094
Cdd:pfam15709 406 EER--KQRLQLQAAQERARQQQEEFRRKLQELQRKKQ-QEEAERAEAEKQRQ---------KELEMQLAEEQK 466
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
442-646 |
5.79e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 442 RKRIKELEEAANKPlEATGLKRnIEEQSQQPKHQSLAQKIYAENR-----RKAEEAHRLMEKlgpKIELPLynqpsdtSV 516
Cdd:PTZ00121 1533 AKKADEAKKAEEKK-KADELKK-AEELKKAEEKKKAEEAKKAEEDknmalRKAEEAKKAEEA---RIEEVM-------KL 1600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 517 YQENRTRHQTCMRTRLIARLRRDHTERASLHQQQTQTYTILVQEWHRKVERL----EATQKRKSKETKNREFFEKVFPEL 592
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELkkaeEENKIKAAEEAKKAEEDKKKAEEA 1680
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1418074753 593 RKQREDKERFNRVGARIKSEADLEEIMDGLQEQEEETLQDLK-----NSIKACQL-----EDKK 646
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKkaeeeNKIKAEEAkkeaeEDKK 1744
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
395-682 |
5.92e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 395 QTEAISPTLPEPNTQEDALRSTKDELLQQIGKVDREIAKRENQLNMLRKRIKELEEAANKpleatgLKRNIEEQSQQPKH 474
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK------LEEALNDLEARLSH 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 475 QSLaQKIYAEnRRKAEEAHRLMEKlgpkielplynqpsdtsvyqenRTRHqtcmrtrLIARLRRDHTERASLHQ--QQTQ 552
Cdd:TIGR02169 791 SRI-PEIQAE-LSKLEEEVSRIEA----------------------RLRE-------IEQKLNRLTLEKEYLEKeiQELQ 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 553 TYTILVQEwhRKVE---RLEATQKRKSK---ETKNREFFEKvfpELRKQREDKERfnrvgARIKSEADLEEIMDGLQEQE 626
Cdd:TIGR02169 840 EQRIDLKE--QIKSiekEIENLNGKKEEleeELEELEAALR---DLESRLGDLKK-----ERDELEAQLRELERKIEELE 909
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1418074753 627 -------------EETLQDLKNSIKACQLEDKKMRSYAVIPPLLLDAKQRRIAFQnrngllqpEELEAL 682
Cdd:TIGR02169 910 aqiekkrkrlselKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVE--------EEIRAL 970
|
|
| ClassIIa_HDAC_Gln-rich-N |
cd10149 |
Glutamine-rich N-terminal helical domain of various Class IIa histone deacetylases (HDAC4, ... |
1965-2049 |
5.94e-04 |
|
Glutamine-rich N-terminal helical domain of various Class IIa histone deacetylases (HDAC4, HDAC5 and HDCA9); This superfamily consists of a glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDAC9; it is missing in HDAC7. It is referred to as the glutamine-rich domain, and confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors. This domain is able to repress transcription independently of the HDAC's C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.
Pssm-ID: 197397 [Multi-domain] Cd Length: 90 Bit Score: 41.22 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1965 REKELQQQLehrLAVQQHHQHREK----DFQQQEHRLAPQREKDIHvEHARLQIREKDIPHEHRLIHQQREKEIHQQiaa 2040
Cdd:cd10149 5 REQQLQQEL---LALKQQQQIQKQlliaEFQKQHENLTRQHEAQLQ-EHIKQQQEMLAIKQQQELLEKQRKLEQQRQ--- 77
|
....*....
gi 1418074753 2041 QREKEHEHR 2049
Cdd:cd10149 78 EQELEKQRR 86
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1958-2096 |
6.10e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1958 KEEHRLHREKELQQQLEHRLAVQQHHQHREKDFQQQEHRLAPQREKdihVEHARLQIREKDIPHEHRLIHQQREK----- 2032
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE---LEELREELEKLEKLLQLLPLYQELEAleael 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1418074753 2033 --------EIHQQIAAQREKEHEhrlaVQQREKEIQHQEQRLAIQQQRENPHVVGSpIQQHAERLAAQQRER 2096
Cdd:COG4717 142 aelperleELEERLEELRELEEE----LEELEAELAELQEELEELLEQLSLATEEE-LQDLAEELEELQQRL 208
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1922-2073 |
6.63e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1922 REQEIRMQEhrMAEHRLTQQHQRERERERDIVHLREKEEHRlhREKELQQQLEH-RLAVQQHHQHREKDFQQQEHRLAPQ 2000
Cdd:pfam13868 2 RENSDELRE--LNSKLLAAKCNKERDAQIAEKKRIKAEEKE--EERRLDEMMEEeRERALEEEEEKEEERKEERKRYRQE 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1418074753 2001 REKDIHvEHARLQIREkdipHEHRLIHQQREKEIHQQIAAQREKEHEHRLAVQ---QREKEIQHQEQRLAIQQQRE 2073
Cdd:pfam13868 78 LEEQIE-EREQKRQEE----YEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQrqlREEIDEFNEEQAEWKELEKE 148
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1913-2097 |
7.93e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1913 DRYDNNRAFREQEIRMQEHRmaeHRLTQQHQRERererdivHLREkeehrLHREKELQQQLEHRLAVQQHHQHREKDFQQ 1992
Cdd:PRK04863 490 SRSEAWDVARELLRRLREQR---HLAEQLQQLRM-------RLSE-----LEQRLRQQQRAERLLAEFCKRLGKNLDDED 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1993 QEHRLAPQREKDIhvEHARLQIREKDiphEHRLIHQQREKEIHQQIAaqrekehehRLAvQQREKEIQHQE--QRLAIQ- 2069
Cdd:PRK04863 555 ELEQLQEELEARL--ESLSESVSEAR---ERRMALRQQLEQLQARIQ---------RLA-ARAPAWLAAQDalARLREQs 619
|
170 180
....*....|....*....|....*....
gi 1418074753 2070 -QQRENPHVVGSPIQQHAERLAAQQRERD 2097
Cdd:PRK04863 620 gEEFEDSQDVTEYMQQLLERERELTVERD 648
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1914-2091 |
8.16e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.96 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1914 RYDNNRAFREQEIRMQEHRMAEHRLTQQHQRErererdivHLREKEEhRLHREKELQQQLEHRLAVQqhHQhREKDFQQQ 1993
Cdd:TIGR00618 358 RDAHEVATSIREISCQQHTLTQHIHTLQQQKT--------TLTQKLQ-SLCKELDILQREQATIDTR--TS-AFRDLQGQ 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1994 EHRLapqrEKDIHVEHARLQIREKDIPHEHRlihQQREKEIHQQIAAQREKEHEHRLA----VQQREKEI-QHQEQRLAI 2068
Cdd:TIGR00618 426 LAHA----KKQQELQQRYAELCAAAITCTAQ---CEKLEKIHLQESAQSLKEREQQLQtkeqIHLQETRKkAVVLARLLE 498
|
170 180
....*....|....*....|...
gi 1418074753 2069 QQQRENPhVVGSPIQQHAERLAA 2091
Cdd:TIGR00618 499 LQEEPCP-LCGSCIHPNPARQDI 520
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1916-2073 |
1.02e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1916 DNNRAFREQEIRMQEHRMAEHRLTQQHQRERERERDIVHLREKEEHR----LHREKELQQQLEHRLAVQQHHQHREKDFQ 1991
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKkadeLKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1992 QQEHRLAPQREKDIHVEHARLQIREKDIPHEhrlihQQREKEIHQQIAAQREKEHEHRLAVQQREKEiQHQEQRLAIQQQ 2071
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-----EAKKAEEAKIKAEELKKAEEEKKKVEQLKKK-EAEEKKKAEELK 1653
|
..
gi 1418074753 2072 RE 2073
Cdd:PTZ00121 1654 KA 1655
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1922-2097 |
1.30e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 43.87 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1922 REQEIRMQEHRMAEHR----LTQQHQRERERERDIVHLREKEEHRLHREKELQQQLEHRLAVQQHHQ--HREKDFQQQEH 1995
Cdd:pfam15558 70 RKARLGREERRRADRRekqvIEKESRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELqaLREQNSLQLQE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1996 RLA-PQREKDIHVEHARLQIREKDipHEHRLIHQQREKEIHQQIAAQR-------EKEHEHRLAVQQREKEIQHQEQR-- 2065
Cdd:pfam15558 150 RLEeACHKRQLKEREEQKKVQENN--LSELLNHQARKVLVDCQAKAEEllrrlslEQSLQRSQENYEQLVEERHRELRek 227
|
170 180 190
....*....|....*....|....*....|....*..
gi 1418074753 2066 -----LAIQQQREnphVVGSPIQQHAERLAAQQRERD 2097
Cdd:pfam15558 228 aqkeeEQFQRAKW---RAEEKEEERQEHKEALAELAD 261
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
411-576 |
1.51e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 411 DALRSTKDELLQQIGKVDREIAKRENQLNMLRKRIKELEEAankpLEATGLKR--NIEEQSQQpkhqslAQKIYAENRRK 488
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ----IRGNGGDRleQLEREIER------LERELEERERR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 489 AEEAHRLMEKLGpkieLPLynqPSDTSVYQENRTRHQTcMRTRLIARLRRDHTERASLHQQQTQtytiLVQEWHRKVERL 568
Cdd:COG4913 361 RARLEALLAALG----LPL---PASAEEFAALRAEAAA-LLEALEEELEALEEALAEAEAALRD----LRRELRELEAEI 428
|
....*...
gi 1418074753 569 EATQKRKS 576
Cdd:COG4913 429 ASLERRKS 436
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
411-637 |
1.59e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 411 DALRSTKDELLQQIGKVDREIAKRENQLNMLRKRIKELEEAankpleatgLKRNIEEQSQQPKHQSLAQKIYAENRRKAE 490
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER---------LEELEEELAELEEELEELEEELEELEEELE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 491 EAHRLMEKLGPKIELplynqpSDTSVYQENRTRHQTcmRTRLIARLRRDHTERASLHQQQTQTYTILVQEWHRKVERLEA 570
Cdd:COG1196 348 EAEEELEEAEAELAE------AEEALLEAEAELAEA--EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1418074753 571 TQKRKSKETKNREFFEKVFPELRKQREDKERFNRVGARIKSEADLEEIMDGLQEQEEETLQDLKNSI 637
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1927-2097 |
1.59e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1927 RMQEHRMAEHRLTQQH---QRERERERDiVHLREKEE-HRLHREKELQ-QQLEHRLAvqqhhQHREKdfqqqeHRLAPQR 2001
Cdd:pfam07888 35 RLEECLQERAELLQAQeaaNRQREKEKE-RYKRDREQwERQRRELESRvAELKEELR-----QSREK------HEELEEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 2002 EKDIHVEHARLQiREKDIPHEHRLIHQQREKEIHQQIAA------------QREKEHEHRLAVQQREKEIQHQEQRLAIQ 2069
Cdd:pfam07888 103 YKELSASSEELS-EEKDALLAQRAAHEARIRELEEDIKTltqrvleretelERMKERAKKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190
....*....|....*....|....*....|..
gi 1418074753 2070 QQRENPHVVGSPIQQ----HAERLAAQQRERD 2097
Cdd:pfam07888 182 QTEEELRSLSKEFQElrnsLAQRDTQVLQLQD 213
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1919-2088 |
1.84e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1919 RAFREQEIRMQEHRMAEH---RLTQQHQRERERERDIVHLREKEEHRLHREKELQQQLEHRLAVQQHHQHREKDFQQQEH 1995
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEekkKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1996 RLAPQREKDIHVEHARlqireKDIPHEHRLIHQQREKEIHQQIAAQ---REKEHEHRLAVQQR-----EKEIQH---QEQ 2064
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELK-----KKEAEEKKKAEELKKAEEENKIKAEeakKEAEEDKKKAEEAKkdeeeKKKIAHlkkEEE 1767
|
170 180
....*....|....*....|....
gi 1418074753 2065 RLAIQQQRENPHVVGSPIQQHAER 2088
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEK 1791
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
408-664 |
1.85e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 408 TQEDALRSTKDELLQQIGKVDREIAKRENQLNMLRKRIKELEEAANKPLE-ATGLKRNIEEQSQQpkHQSLAQKIYAENR 486
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErRRELEERLEELEEE--LAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 487 RKAEEAHRLmEKLGPKIELplynqpSDTSVYQENRTRHQTcmRTRLIARLRRDHTERASLHQQQTQTYTILVQEwHRKVE 566
Cdd:COG1196 338 ELEELEEEL-EEAEEELEE------AEAELAEAEEALLEA--EAELAEAEEELEELAEELLEALRAAAELAAQL-EELEE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 567 RLEATQKRKSKETKNREffekvfpELRKQREDKERfnrvgARIKSEADLEEIMDGLQEQEEETLQDLKNSIKACQLEDKK 646
Cdd:COG1196 408 AEEALLERLERLEEELE-------ELEEALAELEE-----EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
250
....*....|....*...
gi 1418074753 647 MRSYAVIPPLLLDAKQRR 664
Cdd:COG1196 476 EAALAELLEELAEAAARL 493
|
|
| CCDC66 |
pfam15236 |
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ... |
1922-2060 |
2.78e-03 |
|
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.
Pssm-ID: 434558 [Multi-domain] Cd Length: 154 Bit Score: 40.55 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1922 REQEIRMQEHRMAEhrltqqhqRERERERDIVHLREKEEhRLHrEKELQQQLEhrlavQQHHQHREkdfQQQEHRLAPQR 2001
Cdd:pfam15236 33 RGQNALLDPAQLEE--------RERKRQKALEHQNAIKK-QLE-EKERQKKLE-----EERRRQEE---QEEEERLRRER 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1418074753 2002 EKDI-HVEHARLQIREKDiphEHRLIHQQREKEIHQ--QIAAQREKEHEHRLAVQQREKEIQ 2060
Cdd:pfam15236 95 EEEQkQFEEERRKQKEKE---EAMTRKTQALLQAMQkaQELAQRLKQEQRIRELAEKGHDTS 153
|
|
| F-BAR_PombeCdc15_like |
cd07651 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ... |
411-637 |
2.92e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153335 [Multi-domain] Cd Length: 236 Bit Score: 41.90 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 411 DALRsTKDELL---QQIGKVDREIAKRENQLNmlRKRIKELEEaankpleaTGLKRN-----IEEQSQQPKHQSLAQKIY 482
Cdd:cd07651 16 DSLR-TLEELRsfyKERASIEEEYAKRLEKLS--RKSLGGSEE--------GGLKNSldtlrLETESMAKSHLKFAKQIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 483 AENRRKAEEAHRLMEKLGPKIEL---PLYNQPSDTSVY-QENRTRHQT-CMRTRliarlrrdhteraSLHQQQTQTytil 557
Cdd:cd07651 85 QDLEEKLAAFASSYTQKRKKIQShmeKLLKKKQDQEKYlEKAREKYEAdCSKIN-------------SYTLQSQLT---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 558 vqeWHRKVERLEA--TQKRKSKETKNREFFEKVfpelRKQREDKERFNRvgarikseaDLEEIMDGLQEQEEETLQDLKN 635
Cdd:cd07651 148 ---WGKELEKNNAklNKAQSSINSSRRDYQNAV----KALRELNEIWNR---------EWKAALDDFQDLEEERIQFLKS 211
|
..
gi 1418074753 636 SI 637
Cdd:cd07651 212 NC 213
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1923-2074 |
2.99e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1923 EQEIRMQEHRMAEHRLTQQ--HQRERERERDIVHLREKEEHRLHREKELQQQLEhRLAVQQHHQHREKDFQQQEHRLAPQ 2000
Cdd:TIGR02168 350 KEELESLEAELEELEAELEelESRLEELEEQLETLRSKVAQLELQIASLNNEIE-RLEARLERLEDRRERLQQEIEELLK 428
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1418074753 2001 REKDIHVEHARLQIREKDiPHEHRLIHQQREKEihQQIAAQREKEHEHRLAVQQREKEIQHQEQRLAIQQQREN 2074
Cdd:TIGR02168 429 KLEEAELKELQAELEELE-EELEELQEELERLE--EALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
407-499 |
3.05e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 407 NTQEDALRSTKDELLQQIGKVDREIAKRENQLNMLRKRIKELEEAANKPLEATGLKRN-IEEQSQQPKH--------QSL 477
Cdd:PRK12704 53 AIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEeLEKKEKELEQkqqelekkEEE 132
|
90 100 110
....*....|....*....|....*....|.
gi 1418074753 478 AQKIYAENRRK--------AEEA-HRLMEKL 499
Cdd:PRK12704 133 LEELIEEQLQElerisgltAEEAkEILLEKV 163
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
413-643 |
3.05e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 413 LRSTKDELLQQIGKVDREIAKRENQLNMLRKRIKelEEAANKpleATGLKRNIEEQSQQPKHQS-LAQKIYAenRRKAEE 491
Cdd:pfam01576 220 LQEQIAELQAQIAELRAQLAKKEEELQAALARLE--EETAQK---NNALKKIRELEAQISELQEdLESERAA--RNKAEK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 492 AHR-LMEKL-GPKIELPlyNQPSDTSVYQENRTRhqtcmRTRLIARLRRDHTERASLHQQQT----QTYTILVQEWHrkv 565
Cdd:pfam01576 293 QRRdLGEELeALKTELE--DTLDTTAAQQELRSK-----REQEVTELKKALEEETRSHEAQLqemrQKHTQALEELT--- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 566 ERLEATQKRKSKETKNREFFEKVFPELRKQ-------REDKERfnrvgARIKSEADLEEIMDGLQEQEEETlQDLKNSIK 638
Cdd:pfam01576 363 EQLEQAKRNKANLEKAKQALESENAELQAElrtlqqaKQDSEH-----KRKKLEGQLQELQARLSESERQR-AELAEKLS 436
|
....*
gi 1418074753 639 ACQLE 643
Cdd:pfam01576 437 KLQSE 441
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
392-688 |
3.12e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 392 YTPQTEAISPTLPEpnTQEDALRSTKDELLQQigkvdreiakrENQLNMLRKRIKELEEAANKPLEATGLKRNIEE-QSQ 470
Cdd:TIGR00618 209 CTPCMPDTYHERKQ--VLEKELKHLREALQQT-----------QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEElRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 471 QPKHqslaqkiyaENRRKAEEAHRLMEKLGPKIELPLYNQPSDTSVYQENRTRHQTcmRTRLIARLRRDHTERASLHQQQ 550
Cdd:TIGR00618 276 EAVL---------EETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRS--RAKLLMKRAAHVKQQSSIEEQR 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 551 TqtytiLVQEWHRKVERLEatqKRKSKETKNREFFEKVFPE---LRKQREDKERFNRvgaRIKSEADLEEIMDGLQEQEE 627
Cdd:TIGR00618 345 R-----LLQTLHSQEIHIR---DAHEVATSIREISCQQHTLtqhIHTLQQQKTTLTQ---KLQSLCKELDILQREQATID 413
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1418074753 628 ETLQDLKNsikacqLEDKKMRSYAVIPPLLLDAKQRRIAFQNRNGLLQPEELEALHSERKL 688
Cdd:TIGR00618 414 TRTSAFRD------LQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL 468
|
|
| NarQ |
COG3850 |
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ... |
1905-2130 |
3.13e-03 |
|
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];
Pssm-ID: 443059 [Multi-domain] Cd Length: 448 Bit Score: 42.56 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1905 TMADRLLAdrydnnrafREQEIrmqEHRMAEHRLTQQHQRERERERDIVHLREKEEHRLHREKELQQQLEHRLAVQQHHQ 1984
Cdd:COG3850 182 RMADELQE---------LYAEL---EEEEELEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALA 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1985 HREKDFQQQEHRLAPQREKDIHVEHARLQIREKDIPHEHRLIHQQREKEIHQQIAAQREKEHEHRLAVQQREKEIQHQEQ 2064
Cdd:COG3850 250 ESELLALNILAGLLELLLALLLLLLASALLLLELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIANASLL 329
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1418074753 2065 RLAIQQ--QRENPHVVGSPIQQHAERLAAQQRERDLLHLHQQHQQQQQQHMQHIQHQQRIEIERRHIA 2130
Cdd:COG3850 330 LIALASvvAALLELASILALQAALEAAAAGAALAAAAAAAGLARALAQAGADAAEALGLLAEASEGAA 397
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1922-2049 |
3.19e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.18 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1922 REQEIRMQEHRMAEHRLTQQhQRERERERDIVHLREKEEHRLhreKELQQQLEHRLAVQQHHqhrekdFQQQEHRLAPQR 2001
Cdd:cd16269 177 QSKEAEAEAILQADQALTEK-EKEIEAERAKAEAAEQERKLL---EEQQRELEQKLEDQERS------YEEHLRQLKEKM 246
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1418074753 2002 EKDIhvehaRLQIREKDIPHEHRLIHQQR--EKEIHQQIAAQREKEHEHR 2049
Cdd:cd16269 247 EEER-----ENLLKEQERALESKLKEQEAllEEGFKEQAELLQEEIRSLK 291
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1247-1676 |
3.22e-03 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 42.98 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1247 SSDTASAGSPATTMTGSNAAVIPSGGPTATSSSLSfqRPNELGSleklgeriadVTVVSLVPPAGSSHQSSSSGGAAATS 1326
Cdd:pfam05109 440 AAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVT--SPTPAGT----------TSGASPVTPSPSPRDNGTESKAPDMT 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1327 GGaredydSSATETADEgqggadlDNGSVVVTMTTASGNATSLQQQSQQQSQHQQQPPTTAHSP-PSTTSNSNPLTVKDL 1405
Cdd:pfam05109 508 SP------TSAVTTPTP-------NATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPtPAVTTPTPNATIPTL 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1406 mlgviemqlkrTPNSPADGGGSSAPNSSgTPTISSilKTDHRNDITYVRGYKSSSNMTNTalPSRDtnlATLSVVSGPHH 1485
Cdd:pfam05109 575 -----------GKTSPTSAVTTPTPNAT-SPTVGE--TSPQANTTNHTLGGTSSTPVVTS--PPKN---ATSAVTTGQHN 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1486 GHRSAPSPQQI--SQMQATITpcpPAAPSNQGSSSDLL----PKEGLVVMQVQQALRETEgTLDLSIKKPR-----LQQD 1554
Cdd:pfam05109 636 ITSSSTSSMSLrpSSISETLS---PSTSDNSTSHMPLLtsahPTGGENITQVTPASTSTH-HVSTSSPAPRpgttsQASG 711
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1555 YNHSIQLHKPPTVTLYRPEPPPGAyyhphTTPHPEQGRNAKSPLVYASAPRPQASITPKMNKVTVPQTHPKLSPKLGSMS 1634
Cdd:pfam05109 712 PGNSSTSTKPGEVNVTKGTPPKNA-----TSPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDS 786
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1418074753 1635 -TPGHKGGSITHGTPVSTARyeglLRQMTPPGNPPVSGASANV 1676
Cdd:pfam05109 787 tTPRTRYNATTYLPPSTSSK----LRPRWTFTSPPVTTAQATV 825
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1907-2072 |
4.04e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 42.36 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1907 ADRLLADRYDNNRAFREQEIRMQ-EHRMAEHRLtQQHQRERERERDIVHLREKEEHRLH---------------REKELQ 1970
Cdd:pfam19220 123 LERQLAAETEQNRALEEENKALReEAQAAEKAL-QRAEGELATARERLALLEQENRRLQalseeqaaelaeltrRLAELE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1971 QQL----------EHRLAVQQH------HQHrEKDFQQQEHRLAPQREKdIHVEHARLQIREKdIPHEHRliHQQREKEI 2034
Cdd:pfam19220 202 TQLdatrarlralEGQLAAEQAereraeAQL-EEAVEAHRAERASLRMK-LEALTARAAATEQ-LLAEAR--NQLRDRDE 276
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1418074753 2035 HQQIAAQREKEHEHRLAVQQR-----EKEIQHQEQRLA-IQQQR 2072
Cdd:pfam19220 277 AIRAAERRLKEASIERDTLERrlaglEADLERRTQQFQeMQRAR 320
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
402-648 |
4.04e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 402 TLPEPNTQEDALRSTKDELLQQIGKVDREIAKRENQLNMLRKRIKELE-EAANKPLEATGLKRNIEEQsqqpkhqslAQK 480
Cdd:PRK02224 503 DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEaEAEEKREAAAEAEEEAEEA---------REE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 481 IYAENRRKAEEAHRLmEKLgpkielplynqpsdtsvyqeNRTRHQTCMRTRLIARLRRDHTERASLHQQQTQTYTILVQE 560
Cdd:PRK02224 574 VAELNSKLAELKERI-ESL--------------------ERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 561 WHRKVE--------RLEATQKRKSKETknrEFFEKVFPELRKQREDKERF-NRVGArIKSEAD-LEEIMDGLQEQEE--E 628
Cdd:PRK02224 633 RERKREleaefdeaRIEEAREDKERAE---EYLEQVEEKLDELREERDDLqAEIGA-VENELEeLEELRERREALENrvE 708
|
250 260
....*....|....*....|
gi 1418074753 629 TLQDLKNsiKACQLEDKKMR 648
Cdd:PRK02224 709 ALEALYD--EAEELESMYGD 726
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
413-634 |
4.26e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 413 LRSTKDELLQQIGKVDREIAKRENQLNM----------LRKRIKELEEA-ANKPL----------EATGLKRNIEEQSQQ 471
Cdd:COG1340 76 LKEERDELNEKLNELREELDELRKELAElnkaggsidkLRKEIERLEWRqQTEVLspeeekelveKIKELEKELEKAKKA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 472 PKHQSLAQKIYAEN---RRKAEEAHRLMEKLGPKIelplyNQPSD--TSVYQEnrtrhqtcmrtrlIARLRRdhtERASL 546
Cdd:COG1340 156 LEKNEKLKELRAELkelRKEAEEIHKKIKELAEEA-----QELHEemIELYKE-------------ADELRK---EADEL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 547 HQQqtqtytilVQEWHRKVERLEATQKRKSKETknREFFEkvfpELRKQREDKERFNRVGARIKSEADLEEIMDGLQEQE 626
Cdd:COG1340 215 HKE--------IVEAQEKADELHEEIIELQKEL--RELRK----ELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGE 280
|
....*...
gi 1418074753 627 EETLQDLK 634
Cdd:COG1340 281 KLTTEELK 288
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1866-2045 |
4.28e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.89 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1866 ILDAFSNLVEVAIKQPTLPVPhqhghppsgsGGHEgLGKTMADRLLADRYDN-NRAFREQEIR---MQEHRMAEHRLTQQ 1941
Cdd:pfam02841 127 LLQDLSEPLEEKISQGTFSKP----------GGYK-LFLEERDKLEAKYNQVpRKGVKAEEVLqefLQSKEAVEEAILQT 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1942 HQRERERERDIVHLREKEEHRlhrEKELQQQLEHRLAVQQHHQHREKDFQQQEHRLAPQREKDihvehARLQIREKDIPH 2021
Cdd:pfam02841 196 DQALTAKEKAIEAERAKAEAA---EAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEAE-----REQLLAEQERML 267
|
170 180
....*....|....*....|....*
gi 1418074753 2022 EHRLIHQQRE-KEIHQQIAAQREKE 2045
Cdd:pfam02841 268 EHKLQEQEELlKEGFKTEAESLQKE 292
|
|
| Myb_DNA-bind_7 |
pfam15963 |
Myb DNA-binding like; |
1156-1221 |
4.64e-03 |
|
Myb DNA-binding like;
Pssm-ID: 464956 [Multi-domain] Cd Length: 85 Bit Score: 38.29 E-value: 4.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1418074753 1156 SRPWTDEELEQLRKALREYGTNWPKIAEQIPGKTSQQCKNYY------------FAYRKKLSFDQvvSEYYTLLGEER 1221
Cdd:pfam15963 8 TKRWSKEETELFYKALSMFGTDFSLIAQLFPGRTRRQIKLKFkreerknpelvdKALKNRKPFDL--EEFKRLLEKEK 83
|
|
| SANT_MTA3_like |
cd11661 |
Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family ... |
692-735 |
4.91e-03 |
|
Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family include domains found in mouse metastasis-associated protein 3 (MTA3) proteins and arginine-glutamic dipeptide (RERE) repeats proteins. SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domains are a diverse set of proteins that share a common 3 alpha-helix bundle. MTA3 has been shown to interact with nucleosome remodeling and deacetylase (NuRD) proteins CHD4 and HDAC1, and the core cohesin complex protein RAD21 in the ovary, and regulate G2/M progression in proliferating granulosa cells. RERE belongs to the atrophin family and has been identified as a nuclear receptor corepressor; altered expression levels of RERE are associated with cancer in humans while mutations of Rere in mice cause failure in closing the anterior neural tube and fusion of the telencephalic and optic vesicles during embryogenesis.
Pssm-ID: 212559 [Multi-domain] Cd Length: 46 Bit Score: 37.21 E-value: 4.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1418074753 692 WSSVEHESFKEKYLQHPKNYGVIAQS-LEHKGVQDCVHHYYLTKK 735
Cdd:cd11661 2 WSESEAKLFEEGLRKYGKDFHDIRQDfLPWKSVGELVEFYYMWKK 46
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1904-2064 |
5.32e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1904 KTMADRLLADRydNNRAFREQEIRMQEHRMAEHRLTQQHQRE-RERERDIvhlrekeehrlhrekelqQQLEHRLavQQH 1982
Cdd:PRK12704 37 EEEAKRILEEA--KKEAEAIKKEALLEAKEEIHKLRNEFEKElRERRNEL------------------QKLEKRL--LQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1983 HQ---HREKDFQQQEHRLApQREKDIHVEHARLQIREKDIpheHRLIHQQREK----------EIHQQIAAQREKEHEHR 2049
Cdd:PRK12704 95 EEnldRKLELLEKREEELE-KKEKELEQKQQELEKKEEEL---EELIEEQLQElerisgltaeEAKEILLEKVEEEARHE 170
|
170
....*....|....*
gi 1418074753 2050 LAVQQREKEIQHQEQ 2064
Cdd:PRK12704 171 AAVLIKEIEEEAKEE 185
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1911-2089 |
6.78e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1911 LADRYDNNRafreQEIRMQEHRMAEHRLTQQHQRERERERDIVHLREKEEHRLHREKELQQQL-----EHRLAVQQHHQH 1985
Cdd:COG4913 260 LAERYAAAR----ERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLdalreELDELEAQIRGN 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1986 ---REKDFQQQEHRLapQREKDiHVEHARLQIREK------DIPHE-------HRLIHQQREkEIHQQIAAQREKEHEHR 2049
Cdd:COG4913 336 ggdRLEQLEREIERL--ERELE-ERERRRARLEALlaalglPLPASaeefaalRAEAAALLE-ALEEELEALEEALAEAE 411
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1418074753 2050 LAVQQREKEIQHQEQRLAIQQQRenphvvGSPIQQHAERL 2089
Cdd:COG4913 412 AALRDLRRELRELEAEIASLERR------KSNIPARLLAL 445
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1919-2097 |
6.84e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1919 RAFREQEIRMQEHRMAEHRLTQQHQRERERERDIVHLREKEEHRLHREKELQQQLEHRLAVQQHHQHREKDFQQQEHRLA 1998
Cdd:COG1196 601 VDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1999 PQREKDIHVEHARLQIREKDIphEHRLIHQQREKEIHQQIAAQREKEHEHRLAVQQREKEIQHQEQRLAIQQQRENPHVV 2078
Cdd:COG1196 681 LEELAERLAEEELELEEALLA--EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
170
....*....|....*....
gi 1418074753 2079 GSPIQQHAERLAAQQRERD 2097
Cdd:COG1196 759 PPDLEELERELERLEREIE 777
|
|
| REB1 |
COG5147 |
Myb superfamily proteins, including transcription factors and mRNA splicing factors ... |
1158-1197 |
7.95e-03 |
|
Myb superfamily proteins, including transcription factors and mRNA splicing factors [Transcription / RNA processing and modification / Cell division and chromosome partitioning];
Pssm-ID: 227476 [Multi-domain] Cd Length: 512 Bit Score: 41.31 E-value: 7.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1418074753 1158 PWTDEELEQLRKALREYGTNWPKIAEQIPGKTSQQCKNYY 1197
Cdd:COG5147 74 NWSEEEDEQLIDLDKELGTQWSTIADYKDRRTAQQCVERY 113
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
1250-1637 |
7.96e-03 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 41.48 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1250 TASAGSPATTMTGSNAAVIPSGGPTATSSSlsfqRPNELGSLEKLGERIADVTVVSLVPPAGSSHQSSSSGGAAATSGGA 1329
Cdd:pfam17823 63 ATAAPAPVTLTKGTSAAHLNSTEVTAEHTP----HGTDLSEPATREGAADGAASRALAAAASSSPSSAAQSLPAAIAALP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1330 REDYDSSATE---TADEGQGGADLDNGSVVVTMTTASGNATSLQQQSQQQSQHQQQPPTTAHSPPSTTSNSNPLTVKDLM 1406
Cdd:pfam17823 139 SEAFSAPRAAacrANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGISTAATA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1407 LG--VIEMQLKRTPNSPADGGGSSAPNSSGTPTISSILKTDHRNDITYVRGYKSSSNMTNTALPSRDTNLATLSVvsgph 1484
Cdd:pfam17823 219 TGhpAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGDPHARRLSPAKHMPSDTMAR----- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 1485 hghrsapspqqisqmqatiTPCPPAAPSNQGSSSDLlpkeglvvmQVQQALRETEGTLDLSIKKPRLQQDYNHSIQLHKP 1564
Cdd:pfam17823 294 -------------------NPAAPMGAQAQGPIIQV---------STDQPVHNTAGEPTPSPSNTTLEPNTPKSVASTNL 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1418074753 1565 PTVTLYR---PEPPPGAYYHPHTTPHPEqgrnaksplVYASAPRPQASITPKMNKVTVPQThPKLSPKLGSMSTPG 1637
Cdd:pfam17823 346 AVVTTTKaqaKEPSASPVPVLHTSMIPE---------VEATSPTTQPSPLLPTQGAAGPGI-LLAPEQVATEATAG 411
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
423-630 |
8.76e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 423 QIGKVDREIAKRENQLNMLRKRIKELEEAANkplEATGLKRNIEEQSQ-----QPKHQSLAQKIyaENRRKAEEAHRL-M 496
Cdd:pfam01576 132 KIKKLEEDILLLEDQNSKLSKERKLLEERIS---EFTSNLAEEEEKAKslsklKNKHEAMISDL--EERLKKEEKGRQeL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418074753 497 EKLGPKIElplynqpSDTSVYQEnrtrhQTCMRTRLIARLRrdhteraslhqqqtqtytilvQEWHRKVERLEATQKRKS 576
Cdd:pfam01576 207 EKAKRKLE-------GESTDLQE-----QIAELQAQIAELR---------------------AQLAKKEEELQAALARLE 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1418074753 577 KETKNREFFEKVFPELRKQ----REDKErfNRVGARIKSEA---DLEEIMDGLQEQEEETL 630
Cdd:pfam01576 254 EETAQKNNALKKIRELEAQiselQEDLE--SERAARNKAEKqrrDLGEELEALKTELEDTL 312
|
|
| |
