|
Name |
Accession |
Description |
Interval |
E-value |
| DUF3668 |
pfam12416 |
Cep120 protein; This family includes the Cep120 protein which is associated with centriole ... |
118-340 |
6.11e-127 |
|
Cep120 protein; This family includes the Cep120 protein which is associated with centriole structure and function.
Pssm-ID: 463569 Cd Length: 226 Bit Score: 382.06 E-value: 6.11e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 118 KYTKFKSEIQISIALETDTKPP---VDSFKAKGAPPRDGKVPAILAGLDPRDIVAVLNEEGGYHQIGPAEYCTDSFIMSV 194
Cdd:pfam12416 1 KYTKQKPELLLSLALEKDSKPHtkdFDSFKAKPAPPRQSPGHSILANLLPSKLIPYLNEEEGYHQIGPADLCCDIFVLSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 195 TIAFATQLEQLIPCTMKLPERQPEFFFYYSLLGNDVTNEPFNDLINPNFEPERASVRIRSSVEILRVYLALQSKLQIHLC 274
Cdd:pfam12416 81 TIAFATNLEQLVPSSMKLPEEKPGFFFYYSLLGNDVTNEPFKNLLNPNFEPERASVRIRSSLRVLRAYLSSQPYLQIHLC 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1769843751 275 CGDQSLGSTEIPLTGLLKKGSTEINQHPVTVEGAFTLDPPNRAKQKLAPIPVELAPTVGVSVALQR 340
Cdd:pfam12416 161 CGNQSLGSTEVSLQGLLPDNSTELERKPVTIEGAFVLNPPNRAKQDLPEVPLELKPTVGVTVTLRR 226
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
669-913 |
9.68e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.29 E-value: 9.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 669 ENQL----KQKELAH-MQALAEEWKKRDRERESLVKKKV-AEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQS 742
Cdd:COG1196 199 ERQLepleRQAEKAErYRELKEELKELEAELLLLKLRELeAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 743 ERQRnLQELQDSIRRAK---EDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQnnkpeIRLQSE 819
Cdd:COG1196 279 LELE-LEEAQAEEYELLaelARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-----EEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 820 INLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQR--EQESQMARLKKQQEELEQMRLRYLAA--EEKDTVKT 895
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAaaELAAQLEELEEAEEALLERLERLEEEleELEEALAE 432
|
250
....*....|....*...
gi 1769843751 896 ERQELLDIRNELNSDIKK 913
Cdd:COG1196 433 LEEEEEEEEEALEEAAEE 450
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
649-909 |
1.90e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 649 LEYKAALELEMWKEMQEDIFENQLK--QKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEG---KLQKTLIDLEKRE 723
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEelEAELAELEAELEELRLELEELELELEEAQAEEYELLAelaRLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 724 QQLASVESELQREKKELQsERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQ 803
Cdd:COG1196 312 RELEERLEELEEELAELE-EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 804 FKDQQnnkpeIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEELEQMRLR 883
Cdd:COG1196 391 ALRAA-----AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260
....*....|....*....|....*.
gi 1769843751 884 YLAAEEKDTVKTERQELLDIRNELNS 909
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAA 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
675-915 |
6.63e-12 |
|
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: 69.71 E-value: 6.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 675 KELAHMQALAEEWKKRDRERESLVKKKvaeyTILEGKLQKTLIDLEKREQQLASVESELQR--EKKELQSERQRNLQELQ 752
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSEL----RRIENRLDELSQELSDASRKIGEIEKEIEQleQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 753 DSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKY-----KILEKEFQQFKDQ--QNNKPEIRLQSEINLLTL 825
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEvsRIEARLREIEQKLNRLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 826 EKVELERKLESATKSKLHYKQQWG--RALKELARLKQREQESQMARLKKQQEELEQmRLRYLaAEEKDTVKTERQELLDI 903
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKEQIKsiEKEIENLNGKKEELEEELEELEAALRDLES-RLGDL-KKERDELEAQLRELERK 904
|
250
....*....|..
gi 1769843751 904 RNELNSDIKKTN 915
Cdd:TIGR02169 905 IEELEAQIEKKR 916
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
640-902 |
1.43e-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: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 640 EIQTEPRETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYtiLEGKLQKTLIDL 719
Cdd:pfam13868 95 EKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEY--LKEKAEREEERE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 720 EKREQQLASVESELQREKKELQSERQRnlQELQDSIRRAKEDCIHQVElERLKIKQLEEDKHRLQQQLNDAENKYKILEK 799
Cdd:pfam13868 173 AEREEIEEEKEREIARLRAQQEKAQDE--KAERDELRAKLYQEEQERK-ERQKEREEAEKKARQRQELQQAREEQIELKE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 800 EFQQFkdqqnnkpEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQwgralkELAR--LKQREQESQMARLKKQQEEL 877
Cdd:pfam13868 250 RRLAE--------EAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL------EHRRelEKQIEEREEQRAAEREEELE 315
|
250 260
....*....|....*....|....*
gi 1769843751 878 EQMRLRYLAAEEKDTVKTERQELLD 902
Cdd:pfam13868 316 EGERLREEEAERRERIEEERQKKLK 340
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
652-921 |
1.58e-11 |
|
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: 68.56 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 652 KAALELEmwkEMQEDIFENQLKQKELA-HMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVE 730
Cdd:TIGR02169 174 KALEELE---EVEENIERLDLIIDEKRqQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 731 SELQREKKELQ------SERQRNLQELQDSIRRAKEDCIHQVeleRLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQf 804
Cdd:TIGR02169 251 EELEKLTEEISelekrlEEIEQLLEELNKKIKDLGEEEQLRV---KEKIGELEAEIASLERSIAEKERELEDAEERLAK- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 805 kdqqnnkpeirLQSEINLLTLEKVELERKLESATKSklhyKQQWGRALKEL--------ARLKQREQESQMAR--LKKQQ 874
Cdd:TIGR02169 327 -----------LEAEIDKLLAEIEELEREIEEERKR----RDKLTEEYAELkeeledlrAELEEVDKEFAETRdeLKDYR 391
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1769843751 875 EELEQMR-----LRYLAAEEKDTVKTERQELLDIRNELNSDIKKTNTVATVA 921
Cdd:TIGR02169 392 EKLEKLKreineLKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
670-908 |
1.60e-11 |
|
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: 68.54 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 670 NQLKQKELAhmqALAEEWKKRDRERESLvKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQSErqrnLQ 749
Cdd:TIGR02168 220 AELRELELA---LLVLRLEELREELEEL-QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE----LY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 750 ELQDSIRRAKEDCIHQVElerlKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNnkpeiRLQSEINLLTLEKVE 829
Cdd:TIGR02168 292 ALANEISRLEQQKQILRE----RLANLERQLEELEAQLEELESKLDELAEELAELEEKLE-----ELKEELESLEAELEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 830 LERKLESATKSKLHYKQQWGRALKELARLKQRE--QESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNEL 907
Cdd:TIGR02168 363 LEAELEELESRLEELEEQLETLRSKVAQLELQIasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL 442
|
.
gi 1769843751 908 N 908
Cdd:TIGR02168 443 E 443
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
640-884 |
1.67e-11 |
|
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: 68.54 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 640 EIQTEPRETLEYKAALELEMwKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDL 719
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEV-SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 720 EKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDcihQVELERL--KIKQLEEDKHRLQQQLNDAENKYKIL 797
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL---EEQLETLrsKVAQLELQIASLNNEIERLEARLERL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 798 EKEFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQ--ESQMARLKKQQE 875
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDaaERELAQLQARLD 492
|
....*....
gi 1769843751 876 ELEQMRLRY 884
Cdd:TIGR02168 493 SLERLQENL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
709-913 |
4.00e-11 |
|
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: 67.39 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 709 EGKLQKTLIDLEKREQQLASVESELqrEKKELQSERQRNLQELQDSIRRAkedcihQVELERLKIKQLEEDKHRLQQQLN 788
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQL--KSLERQAEKAERYKELKAELREL------ELALLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 789 DAENKYKILEKEFQQfkdqqnnkpeirLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQ--ESQ 866
Cdd:TIGR02168 250 EAEEELEELTAELQE------------LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlERQ 317
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1769843751 867 MARLKKQQEELEQMRLRYlaAEEKDTVKTERQELLDIRNELNSDIKK 913
Cdd:TIGR02168 318 LEELEAQLEELESKLDEL--AEELAELEEKLEELKEELESLEAELEE 362
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
666-900 |
5.64e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 666 DIFENQLKQKElAHMQALAEEWKKRDRERESLVKKKVAEYTILEgkLQKTLIDLEKREQQLASVESELQR------EKKE 739
Cdd:COG4913 613 AALEAELAELE-EELAEAEERLEALEAELDALQERREALQRLAE--YSWDEIDVASAEREIAELEAELERldassdDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 740 LQSERQRnLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKI-----LEKEFQQFKDQQNNKpEI 814
Cdd:COG4913 690 LEEQLEE-LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralLEERFAAALGDAVER-EL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 815 R--LQSEINLLTLEKVELERKLESATKSklhYKQQW--------------GRALKELARLKQR---EQESQMARLKKQQE 875
Cdd:COG4913 768 RenLEERIDALRARLNRAEEELERAMRA---FNREWpaetadldadleslPEYLALLDRLEEDglpEYEERFKELLNENS 844
|
250 260
....*....|....*....|....*
gi 1769843751 876 ELEQMRLRYLAAEEKDTVKTERQEL 900
Cdd:COG4913 845 IEFVADLLSKLRRAIREIKERIDPL 869
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
660-913 |
9.42e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 9.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 660 WKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERE---SLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQRE 736
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEkelEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 737 KKELQSERQrNLQELQDSIRRAKEdcihQVELERLKIKQLEEDKHRLQQQLNDAEnKYKILEKEFQQFKDQQNN--KPEI 814
Cdd:PRK03918 244 EKELESLEG-SKRKLEEKIRELEE----RIEELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREieKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 815 RLQSEINLLTLEKVELERKLESATKSKLHYKQqwgrALKELARLKQREQESQMARLKKqqEELEQMRLRyLAAEEKDTVK 894
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKE----LEKRLEELEERHELYEEAKAKK--EELERLKKR-LTGLTPEKLE 390
|
250
....*....|....*....
gi 1769843751 895 TERQELLDIRNELNSDIKK 913
Cdd:PRK03918 391 KELEELEKAKEEIEEEISK 409
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
654-894 |
1.85e-10 |
|
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: 64.76 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 654 ALELEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQktlidlEKREQQLASVESEL 733
Cdd:pfam17380 371 AMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE------EARQREVRRLEEER 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 734 QREK---KELQSERQRNLQEL--QDSIRRAKEDCIH-----QVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQ 803
Cdd:pfam17380 445 AREMervRLEEQERQQQVERLrqQEEERKRKKLELEkekrdRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 804 FKDQQNNKPEIRlqseinlltleKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARlkkQQEELEQMRLR 883
Cdd:pfam17380 525 RQKAIYEEERRR-----------EAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMR---QIVESEKARAE 590
|
250
....*....|.
gi 1769843751 884 YLAAEEKDTVK 894
Cdd:pfam17380 591 YEATTPITTIK 601
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
713-894 |
6.85e-10 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 60.32 E-value: 6.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 713 QKTLIDLEKREQQLASVESELQREKKELQsERQRNLQELQDSIRRAKEDcIHQVELER----LKIKQLEEDKHRLQQQLN 788
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELA-ELEDELAALEARLEAAKTE-LEDLEKEIkrleLEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 789 DAENkykilEKEFQQfkdqqnnkpeirLQSEINLLTLEKVELE-------RKLESATKSKLHYKQQWGRALKELARLKQr 861
Cdd:COG1579 84 NVRN-----NKEYEA------------LQKEIESLKRRISDLEdeilelmERIEELEEELAELEAELAELEAELEEKKA- 145
|
170 180 190
....*....|....*....|....*....|...
gi 1769843751 862 EQESQMARLKKQQEELEQMRLRYLAAEEKDTVK 894
Cdd:COG1579 146 ELDEELAELEAELEELEAEREELAAKIPPELLA 178
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
639-913 |
2.09e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 61.53 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 639 SEIQTEPRETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQALAEEwkKRDRERESLVKKKVAEYTILEGKLQKTLID 718
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEE--REKTEKLKVEEEKEEKLKAQEEELRALEEE 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 719 LEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQ-----VELERLKIKQLEEDKHRLQQQLNDAENK 793
Cdd:pfam02463 810 LKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELerleeEITKEELLQELLLKEEELEEQKLKDELE 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 794 YKIL----EKEFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHykqqwGRALKELARLKQREQESQMAR 869
Cdd:pfam02463 890 SKEEkekeEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE-----EADEKEKEENNKEEEEERNKR 964
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1769843751 870 LKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNELNSDIKK 913
Cdd:pfam02463 965 LLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
640-922 |
2.17e-09 |
|
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: 61.61 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 640 EIQTEPRETLEYKAALELEMWKEMQEdifeNQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDL 719
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEER----IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 720 EKREQQLasveSELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERlKIKQLEEDKHRLQQQLNDAENKYKILEK 799
Cdd:TIGR02168 799 KALREAL----DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE-QIEELSEDIESLAAEIEELEELIEELES 873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 800 EFQQFKDQQNNKPEIR---------LQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQR--------- 861
Cdd:TIGR02168 874 ELEALLNERASLEEALallrseleeLSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlseeysltl 953
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 862 -EQESQMARLKKQQEELEQmRLRYL--------------------AAEEKDTVKTERQELLDIRNELNSDIKKTNTVATV 920
Cdd:TIGR02168 954 eEAEALENKIEDDEEEARR-RLKRLenkikelgpvnlaaieeyeeLKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
..
gi 1769843751 921 AF 922
Cdd:TIGR02168 1033 RF 1034
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
730-909 |
6.14e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 730 ESELQREKKELQSERQRNLQELQDSIRRAKEDcIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQN 809
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEE-LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 810 NKPEI----RLQSEINLLTLEKVELERKLE---SATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEELEQMRL 882
Cdd:COG4717 127 LLPLYqeleALEAELAELPERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180
....*....|....*....|....*..
gi 1769843751 883 RYLAAEEKdtVKTERQELLDIRNELNS 909
Cdd:COG4717 207 RLAELEEE--LEEAQEELEELEEELEQ 231
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
660-908 |
6.92e-09 |
|
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: 60.08 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 660 WKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKR----------------- 722
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeiqaelskle 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 723 ------EQQLASVESELQR---EKKELQSERQrNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENK 793
Cdd:TIGR02169 805 eevsriEARLREIEQKLNRltlEKEYLEKEIQ-ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 794 YKILEKEFQQFKDQQNNkpeirLQSEINLLTLEkVELERKLESATKSKLHYKQQwgrALKELARLKQREQES-------- 865
Cdd:TIGR02169 884 LGDLKKERDELEAQLRE-----LERKIEELEAQ-IEKKRKRLSELKAKLEALEE---ELSEIEDPKGEDEEIpeeelsle 954
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1769843751 866 --QMARLKKQQ-------------EELEQMRLRYLAAEEK-DTVKTERQELLDIRNELN 908
Cdd:TIGR02169 955 dvQAELQRVEEeiralepvnmlaiQEYEEVLKRLDELKEKrAKLEEERKAILERIEEYE 1013
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
615-907 |
6.96e-09 |
|
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: 59.75 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 615 ISDSSQGVSAVQQKPSSLPPAPcPSEIQTEPRETLEYKAALELEMW-----KEMQEDIFENQL-----KQKELAHMQAlA 684
Cdd:pfam17380 213 IQMSTVAPKEVQGMPHTLAPYE-KMERRKESFNLAEDVTTMTPEYTvryngQTMTENEFLNQLlhivqHQKAVSERQQ-Q 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 685 EEWKKRDRERESLVKKKVAEytilEGKLQKTLIDLEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIH 764
Cdd:pfam17380 291 EKFEKMEQERLRQEKEEKAR----EVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIR 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 765 QVE----------LERLKIKQlEEDKHRLQQQLnDAENKYKILEKEFQ-----------QFKDQQNNKPEIRLQ--SEIN 821
Cdd:pfam17380 367 QEEiameisrmreLERLQMER-QQKNERVRQEL-EAARKVKILEEERQrkiqqqkvemeQIRAEQEEARQREVRrlEEER 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 822 LLTLEKVELERKLESATKSKLHYKQQWGRALK-ELARLKQREQESQMARLKKQQEELEQMRLRYLaaEEKDTVKTERQEL 900
Cdd:pfam17380 445 AREMERVRLEEQERQQQVERLRQQEEERKRKKlELEKEKRDRKRAEEQRRKILEKELEERKQAMI--EEERKRKLLEKEM 522
|
....*..
gi 1769843751 901 LDIRNEL 907
Cdd:pfam17380 523 EERQKAI 529
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
658-912 |
1.46e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 658 EMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKvAEYTILEGKLQKTLIDLEKREQQLASVESELqREK 737
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL-REIEKRLSRLEEEINGIEERIKELEEKEERL-EEL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 738 KELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIRLQ 817
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 818 SEINLLTLEKVELE-----RKLESATKSKL--HYKQQWGRALKELARLKQREQ---------------ESQMARLKKQQE 875
Cdd:PRK03918 424 LKKAIEELKKAKGKcpvcgRELTEEHRKELleEYTAELKRIEKELKEIEEKERklrkelrelekvlkkESELIKLKELAE 503
|
250 260 270
....*....|....*....|....*....|....*....
gi 1769843751 876 ELEQM--RLRYLAAEEKDTVKTERQELLDIRNELNSDIK 912
Cdd:PRK03918 504 QLKELeeKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
663-901 |
1.47e-08 |
|
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: 58.37 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 663 MQEDIFENQLKQKELAHMQALAEEWKKRDRERESlvkkKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQS 742
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELES----RVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 743 ERQRNLQ---ELQDSIRRAKEDCI-HQVELERLK---------IKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQN 809
Cdd:pfam07888 123 QRAAHEArirELEEDIKTLTQRVLeRETELERMKerakkagaqRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 810 NKPE--IRLQSEINLLTL-------EKVELERKLE--SATKSKLHYKQQ----WGRALKELARLKQREQ-ESQMARLKKQ 873
Cdd:pfam07888 203 QRDTqvLQLQDTITTLTQklttahrKEAENEALLEelRSLQERLNASERkvegLGEELSSMAAQRDRTQaELHQARLQAA 282
|
250 260
....*....|....*....|....*...
gi 1769843751 874 QEELEQMRLRYLAAEEKDTVKTERQELL 901
Cdd:pfam07888 283 QLTLQLADASLALREGRARWAQERETLQ 310
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
656-900 |
3.95e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.44 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 656 ELEMWKEMQEDIFENQLKQKELAHMQaLAEEWKKRDREREslvkkkvaEYTILEGKLQKTLIDLEKREQQLaSVESELQR 735
Cdd:pfam15921 332 ELREAKRMYEDKIEELEKQLVLANSE-LTEARTERDQFSQ--------ESGNLDDQLQKLLADLHKREKEL-SLEKEQNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 736 E---------------KKELqSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKE 800
Cdd:pfam15921 402 RlwdrdtgnsitidhlRREL-DDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKV 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 801 FQQFKDQQnnkpeIRLQSE---INLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQEsqmarLKKQQEEL 877
Cdd:pfam15921 481 VEELTAKK-----MTLESSertVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDH-----LRNVQTEC 550
|
250 260
....*....|....*....|...
gi 1769843751 878 EQMRLRylAAEEKDTVKTERQEL 900
Cdd:pfam15921 551 EALKLQ--MAEKDKVIEILRQQI 571
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
739-917 |
4.41e-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: 56.31 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 739 ELQSERQRNLQELQDSIRRAKEdcihQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQ--QNNKPEIRL 816
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEK----ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 817 QSEINLLtleKVELERKLESATKSKLHYK-------QQWGRALKELARLKQ--REQESQMARLKKQQEELEQmrLRYLAA 887
Cdd:COG4942 96 RAELEAQ---KEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYlaPARREQAEELRADLAELAA--LRAELE 170
|
170 180 190
....*....|....*....|....*....|
gi 1769843751 888 EEKDTVKTERQELLDIRNELNSDIKKTNTV 917
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKL 200
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
661-913 |
4.50e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.95 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 661 KEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKEL 740
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 741 QSERQRNLQeLQDSIRRAKEDcIHQVElerLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKpeirlQSEI 820
Cdd:TIGR04523 429 ERLKETIIK-NNSEIKDLTNQ-DSVKE---LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK-----EKEL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 821 NLLTLEKVELERKLESATK--SKLHYKQ--------QWGRALKELAR-LKQREQESQMARLKKQ----QEELEQMRLRYL 885
Cdd:TIGR04523 499 KKLNEEKKELEEKVKDLTKkiSSLKEKIeklesekkEKESKISDLEDeLNKDDFELKKENLEKEidekNKEIEELKQTQK 578
|
250 260
....*....|....*....|....*...
gi 1769843751 886 AAEEKdtvKTERQELLDIRNELNSDIKK 913
Cdd:TIGR04523 579 SLKKK---QEEKQELIDQKEKEKKDLIK 603
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
691-907 |
4.97e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 691 DRERESLVKKKVAEYTILEGKLQktliDLEKREQQLASVESELQREKKELQSERQRnLQELQDSIRRAKEDcihQVELER 770
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELK----ELEEELKEAEEKEEEYAELQEELEELEEE-LEELEAELEELREE---LEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 771 LK-IKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIRLQSEinlltlekvELERKLESA-TKSKLHYKQQW 848
Cdd:COG4717 124 LLqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA---------ELQEELEELlEQLSLATEEEL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1769843751 849 GRALKELARLKQREQESQmarlkkqqEELEQMRLRYLAAEEKDTVKTERQELLDIRNEL 907
Cdd:COG4717 195 QDLAEELEELQQRLAELE--------EELEEAQEELEELEEELEQLENELEAAALEERL 245
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
673-840 |
5.74e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.55 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 673 KQKELAHMQALAEEWKKRDRERESLvKKKVAEytiLEGKLQKTLIDLEKREQQLASVESELQREKKELQSERQR--NLQE 750
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKEL-PAELAE---LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 751 LQDSIRRAKE--DCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKpEIRLQSEINLLTLEKV 828
Cdd:COG1579 81 QLGNVRNNKEyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK-KAELDEELAELEAELE 159
|
170
....*....|..
gi 1769843751 829 ELERKLESATKS 840
Cdd:COG1579 160 ELEAEREELAAK 171
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
690-910 |
8.22e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 690 RDRERESLV-----KKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQ-----SERQRNLQELQDSIRRAK 759
Cdd:COG4913 595 RRRIRSRYVlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeySWDEIDVASAEREIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 760 EdcihqvELERLK--IKQLEEdkhrLQQQLNDAENKYKILEKEFQQFKDQQnnkpeIRLQSEINLLTLEKVELERKLESA 837
Cdd:COG4913 675 A------ELERLDasSDDLAA----LEEQLEELEAELEELEEELDELKGEI-----GRLEKELEQAEEELDELQDRLEAA 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 838 TKSK-----LHYKQQWGRAL-----KELARLKQREQESQMARLKKQQEELEQMRLRYL-----AAEEKDTVKTERQELLD 902
Cdd:COG4913 740 EDLArlelrALLEERFAAALgdaveRELRENLEERIDALRARLNRAEEELERAMRAFNrewpaETADLDADLESLPEYLA 819
|
....*...
gi 1769843751 903 IRNELNSD 910
Cdd:COG4913 820 LLDRLEED 827
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
718-880 |
1.75e-07 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 55.03 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 718 DLEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDcIHQVELER----LKIKQLEEDKHRLQQQLNDAENK 793
Cdd:pfam05667 307 QFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESS-IQELEKEIkkleSSIKQVEEELEELKEQNEELEKQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 794 YKILEKEFQQFKDQQNNkpeirlqseinlltLEKveLERKLESATKSKLHYKQQWG----------RALKELARLKQREQ 863
Cdd:pfam05667 386 YKVKKKTLDLLPDAEEN--------------IAK--LQALVDASAQRLVELAGQWEkhrvplieeyRALKEAKSNKEDES 449
|
170
....*....|....*..
gi 1769843751 864 ESQMARLKKQQEELEQM 880
Cdd:pfam05667 450 QRKLEEIKELREKIKEV 466
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
640-808 |
4.49e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 640 EIQTEPRETLEYKAALElEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLvkkkvAEYTILEGKLQKTLIDL 719
Cdd:COG4717 85 EKEEEYAELQEELEELE-EELEELEAELEELREELEKLEKLLQLLPLYQELEALEAEL-----AELPERLEELEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 720 EKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEdcihqvELERL--KIKQLEEDKHRLQQQLNDAENKYKIL 797
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE------ELEELqqRLAELEEELEEAQEELEELEEELEQL 232
|
170
....*....|.
gi 1769843751 798 EKEFQQFKDQQ 808
Cdd:COG4717 233 ENELEAAALEE 243
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
642-905 |
9.38e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.05 E-value: 9.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 642 QTEPRETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAE---YTILEGKL---QKT 715
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLerrKVDDEEKLkesEKE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 716 LIDLEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELE---RLKIKQLEEDKHRLQQQLNDAEN 792
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLakkKLESERLSSAAKLKEEELELKSE 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 793 KYKILEKE---FQQFKDQQNN--KPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQEsqm 867
Cdd:pfam02463 403 EEKEAQLLlelARQLEDLLKEekKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL--- 479
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1769843751 868 arlKKQQEELEQMRLRYLAAEE--KDTVKTERQELLDIRN 905
Cdd:pfam02463 480 ---VKLQEQLELLLSRQKLEERsqKESKARSGLKVLLALI 516
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
681-891 |
1.16e-06 |
|
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: 51.69 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 681 QALAEEWKKRDRERESLvKKKVAEytiLEGKLQKTLIDLEKREQQLASVE---SELQREKKELQSErqrnLQELQDSIRR 757
Cdd:COG4942 16 AAQADAAAEAEAELEQL-QQEIAE---LEKELAALKKEEKALLKQLAALErriAALARRIRALEQE----LAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 758 AKEdcihqvELERLKiKQLEEDKHRLQQQLNDAenkYKILEKEFQQFKDQQNNKPEI------------RLQSEINLLTL 825
Cdd:COG4942 88 LEK------EIAELR-AELEAQKEELAELLRAL---YRLGRQPPLALLLSPEDFLDAvrrlqylkylapARREQAEELRA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1769843751 826 EKVELERK---LESATKSKLHYKQQWGRALKELARLKQrEQESQMARLKKQQEELEQmRLRYLAAEEKD 891
Cdd:COG4942 158 DLAELAALraeLEAERAELEALLAELEEERAALEALKA-ERQKLLARLEKELAELAA-ELAELQQEAEE 224
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
689-913 |
1.33e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 52.67 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 689 KRDRERESLVKKKVAEYtilegkLQKTLIDLEKREQQLasvESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVEL 768
Cdd:pfam02463 168 KRKKKEALKKLIEETEN------LAELIIDLEELKLQE---LKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 769 ERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIrlQSEINLLTLEKVELERKLESATKSKLHYKQQW 848
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQ--EEELKLLAKEEEELKSELLKLERRKVDDEEKL 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1769843751 849 GRALKELARLKQREQESQMARLKKQQEELEQMRLRYLAAEEKDtvKTERQELLDIRNELNSDIKK 913
Cdd:pfam02463 317 KESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE--ELEKLQEKLEQLEEELLAKK 379
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
711-913 |
1.35e-06 |
|
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: 51.69 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 711 KLQKTLIDLEKREQQLASVESELQREKKELQSErqrnLQELQDSIRRAKEDcIHQVELErlkIKQLEEDKHRLQQQLNDA 790
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQ----LAALERRIAALARR-IRALEQE---LAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 791 ENKYKILEKEFQQ-----FKDQQNNKPEIRLQSE-----------INLLTLEKVELERKLEsATKSKLHYKQQwgRALKE 854
Cdd:COG4942 96 RAELEAQKEELAEllralYRLGRQPPLALLLSPEdfldavrrlqyLKYLAPARREQAEELR-ADLAELAALRA--ELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1769843751 855 LARLKQREQESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNELNSDIKK 913
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
683-909 |
1.51e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 683 LAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQ------SERQRNLQELQDSIR 756
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEqleeelEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 757 RAKED---CIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQN--NKPEIRLQSEINLLTLEKVELE 831
Cdd:COG4372 84 ELNEQlqaAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAelQSEIAEREEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769843751 832 RKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNELNS 909
Cdd:COG4372 164 EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
646-858 |
1.54e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 646 RETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQ 725
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 726 LASVESELQREKKELQS---------ERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKI 796
Cdd:COG1196 388 LLEALRAAAELAAQLEEleeaeeallERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1769843751 797 LEKEFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARL 858
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
718-913 |
1.82e-06 |
|
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: 51.98 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 718 DLEKREQQLASVESELQREKKELQSErQRNLQELQDSIRRAKEDCIHQVEL-------ERLKIKQLEEDKHRLQQQLNDA 790
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKE-LEELEEELEQLRKELEELSRQISAlrkdlarLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 791 ENKYKI----LEKEFQQFK----DQQNNKPEI-RLQSEINLLTLEKVELERKLeSATKSKLHYKQQWGRALKELARLKQR 861
Cdd:TIGR02168 760 EAEIEEleerLEEAEEELAeaeaEIEELEAQIeQLKEELKALREALDELRAEL-TLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1769843751 862 EQESQMARLKKQQEELEQMRLRYLAAEEK-DTVKTERQELLDIRNELNSDIKK 913
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELiEELESELEALLNERASLEEALAL 891
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
720-899 |
2.67e-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: 51.11 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 720 EKREQQLASVESELQREKKelQSERQRnLQELQDSIRRakedcihqVELERlKIKQLEEDKHRLQQQLNDAENKYKILEK 799
Cdd:pfam15709 313 EERSEEDPSKALLEKREQE--KASRDR-LRAERAEMRR--------LEVER-KRREQEEQRRLQQEQLERAEKMREELEL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 800 EfqqfkdQQNNKPEIRL----QSEINLLTLEKVELERKLESATKSKLHYKQQ-WGRALKELARLKQREQESQMARLKKQQ 874
Cdd:pfam15709 381 E------QQRRFEEIRLrkqrLEEERQRQEEEERKQRLQLQAAQERARQQQEeFRRKLQELQRKKQQEEAERAEAEKQRQ 454
|
170 180 190
....*....|....*....|....*....|.
gi 1769843751 875 EEL------EQMRLRYLAAEEKDTVKTERQE 899
Cdd:pfam15709 455 KELemqlaeEQKRLMEMAEEERLEYQRQKQE 485
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
724-913 |
3.12e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 724 QQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQ 803
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 804 FKDQQNNKPEIRLQSEINLLTLEKV--ELERKLESATKS--KLhykqqwG----RALKELARLKQREQEsqmarLKKQQE 875
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDleELERELERLEREieAL------GpvnlLAIEEYEELEERYDF-----LSEQRE 805
|
170 180 190
....*....|....*....|....*....|....*...
gi 1769843751 876 ELEQmrlrylaaeekdtvktERQELLDIRNELNSDIKK 913
Cdd:COG1196 806 DLEE----------------ARETLEEAIEEIDRETRE 827
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
650-916 |
4.14e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.74 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 650 EYKAALELemwKEMQEDIFENQLKQKELAHmQALAEEWKKRDRERESLVKKKVAEYtiLEGKLQKTLIDLEKREQQLASV 729
Cdd:pfam02463 171 KKEALKKL---IEETENLAELIIDLEELKL-QELKLKEQAKKALEYYQLKEKLELE--EEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 730 ESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEfqqfkdQQN 809
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK------LKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 810 NKPEIRlqseinlltlekvelerKLESATKSKLHYK--QQWGRALKELARLKQREQESQMARL----------------K 871
Cdd:pfam02463 319 SEKEKK-----------------KAEKELKKEKEEIeeLEKELKELEIKREAEEEEEEELEKLqekleqleeellakkkL 381
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1769843751 872 KQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNELNSDIKKTNT 916
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKK 426
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
670-899 |
4.41e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 670 NQLKQKELAHMQA----LAEEWKKRDRERESLVKKKVAEYTILEgklQKTLIDLEKREQQLASVESELQREKKELQSERQ 745
Cdd:PTZ00121 1500 DEAKKAAEAKKKAdeakKAEEAKKADEAKKAEEAKKADEAKKAE---EKKKADELKKAEELKKAEEKKKAEEAKKAEEDK 1576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 746 RNLQELQDSIRRAKEDCIHQV-----ELERLKIKQL--EEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIRLQS 818
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVmklyeEEKKMKAEEAkkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 819 EINllTLEKVELERKLESATKSKlhykqqwgralkELARLKQREQESQMARLKKQQEELEQM-RLRYLAAEEKDTVKTER 897
Cdd:PTZ00121 1657 EEN--KIKAAEEAKKAEEDKKKA------------EEAKKAEEDEKKAAEALKKEAEEAKKAeELKKKEAEEKKKAEELK 1722
|
..
gi 1769843751 898 QE 899
Cdd:PTZ00121 1723 KA 1724
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
725-902 |
4.57e-06 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 48.00 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 725 QLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDK---HR----LQQQLNDAENKYKIL 797
Cdd:pfam08614 11 RLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELaelYRsrgeLAQRLVDLNEELQEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 798 EKEFQQfkdqqnnkpeirLQSEINLLTLEKVELERKLESATksklhykqqwgRALKELARLKQReqesqmarlkkQQEEL 877
Cdd:pfam08614 91 EKKLRE------------DERRLAALEAERAQLEEKLKDRE-----------EELREKRKLNQD-----------LQDEL 136
|
170 180
....*....|....*....|....*.
gi 1769843751 878 EQMRLRYLAAEEK-DTVKTERQELLD 902
Cdd:pfam08614 137 VALQLQLNMAEEKlRKLEKENRELVE 162
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
669-795 |
5.63e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 669 ENQLKQKELahmQAlAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELqSERQRNL 748
Cdd:PRK12704 52 EAIKKEALL---EA-KEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKEL-EQKQQEL 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1769843751 749 QELQDSIRRAKEDciHQVELERLKIKQLEEDKHRLqqqLNDAENKYK 795
Cdd:PRK12704 127 EKKEEELEELIEE--QLQELERISGLTAEEAKEIL---LEKVEEEAR 168
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
669-915 |
5.86e-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: 49.53 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 669 ENQLKQKELAHMQALAEEwKKRDRERESLVKKKVAEYTILEGKLQktlidlEKREQQLASVESELQREKKELQSERQRNL 748
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEE-RRLDEMMEEERERALEEEEEKEEERK------EERKRYRQELEEQIEEREQKRQEEYEEKL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 749 QElqdsiRRAKEDCIHQVELERLKIKQLeedKHRLQQQLNdaenkykileKEFQQFKDQQNNKPEIRLQSEinlltlekV 828
Cdd:pfam13868 98 QE-----REQMDEIVERIQEEDQAEAEE---KLEKQRQLR----------EEIDEFNEEQAEWKELEKEEE--------R 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 829 ELERKLESATKSKLHYKQQWGRALKELARLKQREQE---SQMARLKKQQEELEQMRL-RYLAAEEKDTVKTERQELLDiR 904
Cdd:pfam13868 152 EEDERILEYLKEKAEREEEREAEREEIEEEKEREIArlrAQQEKAQDEKAERDELRAkLYQEEQERKERQKEREEAEK-K 230
|
250
....*....|.
gi 1769843751 905 NELNSDIKKTN 915
Cdd:pfam13868 231 ARQRQELQQAR 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
644-899 |
6.34e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 644 EPRETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKRE 723
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 724 QQLAsveSELQREKKELQSERQRNLQElqdsiRRAKEDCIHQVELERLKIKQL---EEDKHRLQQQLNDAENKYKILEKE 800
Cdd:PTZ00121 1594 IEEV---MKLYEEEKKMKAEEAKKAEE-----AKIKAEELKKAEEEKKKVEQLkkkEAEEKKKAEELKKAEEENKIKAAE 1665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 801 FQQFKDQQNNKPEIRLQSEinlltlekvELERKLESATKSKLHYKQQwgralKELARLKQREQESQMARLKKQQEE--LE 878
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAE---------EDEKKAAEALKKEAEEAKK-----AEELKKKEAEEKKKAEELKKAEEEnkIK 1731
|
250 260
....*....|....*....|.
gi 1769843751 879 QMRLRYLAAEEKDTVKTERQE 899
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKD 1752
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
652-879 |
6.39e-06 |
|
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: 50.17 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 652 KAALELEmWKEMQEDI-------FENQLKQKEL-AHMQALAEEWKKRDRERESLVKKKVAEYTILEGkLQKTLIDLE--- 720
Cdd:pfam01576 379 KQALESE-NAELQAELrtlqqakQDSEHKRKKLeGQLQELQARLSESERQRAELAEKLSKLQSELES-VSSLLNEAEgkn 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 721 -KREQQLASVESELQREKKELQSERQrnlQELQDSIRrakedcihqvelerlkIKQLEEDKHRLQQQLNDAENKYKILEK 799
Cdd:pfam01576 457 iKLSKDVSSLESQLQDTQELLQEETR---QKLNLSTR----------------LRQLEDERNSLQEQLEEEEEAKRNVER 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 800 EFQQFKDQQNnkpEIRLQSEINLLTLEKVELERKlesatksklhykqqwgRALKELARLKQR--EQESQMARLKKQQEEL 877
Cdd:pfam01576 518 QLSTLQAQLS---DMKKKLEEDAGTLEALEEGKK----------------RLQRELEALTQQleEKAAAYDKLEKTKNRL 578
|
..
gi 1769843751 878 EQ 879
Cdd:pfam01576 579 QQ 580
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
664-895 |
6.51e-06 |
|
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: 49.38 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 664 QEDIFENQLKQKEL-AHMQALAEEWKKRDRERESLVK------KKVAEYTILEGKLQKTLIDLEKREQQLASVESELQRE 736
Cdd:COG4942 19 ADAAAEAEAELEQLqQEIAELEKELAALKKEEKALLKqlaaleRRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 737 KKELQSERQRNLQELQDSIRRAKEDCIhqvelerLKIKQLEEDKHRLQ--QQLNDAenkykiLEKEFQQFKDQQNnkpei 814
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALL-------LSPEDFLDAVRRLQylKYLAPA------RREQAEELRADLA----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 815 RLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQR--EQESQMARLKKQQEELEQM--RLRYLAAEEK 890
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKElaELAAELAELQQEAEELEALiaRLEAEAAAAA 240
|
....*
gi 1769843751 891 DTVKT 895
Cdd:COG4942 241 ERTPA 245
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
669-899 |
6.97e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 49.74 E-value: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 669 ENQLKQKELAHMQALAEewkkrdRERESLVKKKVAEYTILEGK-LQKTLIDLEKRE---QQLASVESELQREKKELQSER 744
Cdd:pfam05557 15 QNEKKQMELEHKRARIE------LEKKASALKRQLDRESDRNQeLQKRIRLLEKREaeaEEALREQAELNRLKKKYLEAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 745 QRNLQELQDSIRRAKE--DCI--------HQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQ--NNKP 812
Cdd:pfam05557 89 NKKLNEKESQLADAREviSCLknelselrRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQssLAEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 813 EIRLQseinlltlekvELERKLESATKSKLHYKQqwgrALKELARLKqrEQESQMARLKKQQEELEQM-RLRYLAAEEKD 891
Cdd:pfam05557 169 EQRIK-----------ELEFEIQSQEQDSEIVKN----SKSELARIP--ELEKELERLREHNKHLNENiENKLLLKEEVE 231
|
250
....*....|
gi 1769843751 892 TVKT--ERQE 899
Cdd:pfam05557 232 DLKRklEREE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
677-914 |
7.79e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 677 LAHMQALAEEWKKRDRERESLVKKKvAEYTILEG------KLQKTLIDLEKREQQLASVESELQREKKELQSERQRNLQE 750
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDAR-EQIELLEPirelaeRYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 751 LQDSIRRAKEDCIHQVELERLKIKQLEE--------DKHRLQQQLNDAENKYKILEKEFQQFKDQQNnkpEIRLQseinl 822
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAqirgnggdRLEQLEREIERLERELEERERRRARLEALLA---ALGLP----- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 823 LTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQmARLKKQQEELEQMRLRylaaeeKDTVkteRQELLD 902
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR-RELRELEAEIASLERR------KSNI---PARLLA 444
|
250
....*....|..
gi 1769843751 903 IRNELNSDIKKT 914
Cdd:COG4913 445 LRDALAEALGLD 456
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
671-892 |
8.82e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 8.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 671 QLKQKELAHMQALAEEWKKRDREReslvKKKVAEYTILEGKLQKTLiDLEKREQQLASVESELQREKKELQSERQRNLQE 750
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEE----AKKAEEAKIKAEELKKAE-EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 751 LQDSIRRAKEDCIHQVELerlkiKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIRLQSEINLLTLEkvEL 830
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEEA-----KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE--EA 1735
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1769843751 831 ERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQ---QEELEQMRLRYLAAEEKDT 892
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEaviEEELDEEDEKRRMEVDKKI 1800
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
643-924 |
8.84e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.72 E-value: 8.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 643 TEPRETLEYKAALELEMwKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKR 722
Cdd:pfam05483 391 SELEEMTKFKNNKEVEL-EELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 723 EQQLASVESELQREK----------KELQSERQRNLQELQD---SIRRAKEDCIHQVELERLKIKQLEEdkhrLQQQLND 789
Cdd:pfam05483 470 LKEVEDLKTELEKEKlknieltahcDKLLLENKELTQEASDmtlELKKHQEDIINCKKQEERMLKQIEN----LEEKEMN 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 790 AENKYKILEKEFQQFKDQ--------QNNKPEIR---LQSEINLLTLEKV--ELERKLESATKSkLHYKQQWGRALKELA 856
Cdd:pfam05483 546 LRDELESVREEFIQKGDEvkckldksEENARSIEyevLKKEKQMKILENKcnNLKKQIENKNKN-IEELHQENKALKKKG 624
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769843751 857 RLKQREQESQMARLKKQQEELEQMRLRYlaAEEKDTVKTERQELLDIRNELNSDIKKTNTVATVAFVL 924
Cdd:pfam05483 625 SAENKQLNAYEIKVNKLELELASAKQKF--EEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKL 690
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
639-902 |
9.27e-06 |
|
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: 49.12 E-value: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 639 SEIQTEPRETLEYKAALELEMWKEMQEDIfeNQLKQKELAHMQALaEEWKKRDRERESLVKKKVAEYTILEGKLQKTlid 718
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIRELEEDI--KTLTQRVLERETEL-ERMKERAKKAGAQRKEEEAERKQLQAKLQQT--- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 719 lekrEQQLASVESELQrEKKELQSERQRNLQELQDSIRRA--KEDCIHQVELERlkiKQLEEDKHRLQQQLNDAENKYKI 796
Cdd:pfam07888 184 ----EEELRSLSKEFQ-ELRNSLAQRDTQVLQLQDTITTLtqKLTTAHRKEAEN---EALLEELRSLQERLNASERKVEG 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 797 LEKEFQQFKDQQNnkpeiRLQSEINLLTLEKVELERKLESATKSKLHYKQQWG---------------RALK---ELARL 858
Cdd:pfam07888 256 LGEELSSMAAQRD-----RTQAELHQARLQAAQLTLQLADASLALREGRARWAqeretlqqsaeadkdRIEKlsaELQRL 330
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1769843751 859 KQREQESQMARLKKQQE-----------------ELEQMR--LRyLAAEEKDTVKTERQELLD 902
Cdd:pfam07888 331 EERLQEERMEREKLEVElgrekdcnrvqlsesrrELQELKasLR-VAQKEKEQLQAEKQELLE 392
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
652-830 |
1.01e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 652 KAALELEMWKEMQE--DIFENQLKQKEL-AHMQALAEEWKKRDRERESLVKKKVAeytiLEGKLQKTLIDLEKRE-QQLA 727
Cdd:COG4913 266 AARERLAELEYLRAalRLWFAQRRLELLeAELEELRAELARLEAELERLEARLDA----LREELDELEAQIRGNGgDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 728 SVESELQREKKELQsERQRNLQELQDSIR--------------RAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENK 793
Cdd:COG4913 342 QLEREIERLERELE-ERERRRARLEALLAalglplpasaeefaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1769843751 794 YKILEKEFQQFKDQQNNKPE--IRLQSEIN-LLTLEKVEL 830
Cdd:COG4913 421 LRELEAEIASLERRKSNIPArlLALRDALAeALGLDEAEL 460
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
616-896 |
1.14e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.10 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 616 SDSSQGVSAVQQKPSSLPPAPCPSEIQTEPRETLEYKAALELEMWK---EMQEDIFENQLKQKELAHMQALAEE-WKKRD 691
Cdd:pfam02029 25 EEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKreeRRQKRLQEALERQKEFDPTIADEKEsVAERK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 692 RERESLVKKKVAEYTILEGKLQKTLID----LEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVE 767
Cdd:pfam02029 105 ENNEEEENSSWEKEEKRDSRLGRYKEEeteiREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 768 LERLKIKqlEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIRLQS-EINLLTLEKVELERKLESATKS------ 840
Cdd:pfam02029 185 KKEKKVK--YESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSqEREEEAEVFLEAEQKLEELRRRrqekes 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1769843751 841 ----KLHYKQQwgRALKELARLKQREQESQMA-----RLKKQQEELEQMRLRylaaEEKDTVKTE 896
Cdd:pfam02029 263 eefeKLRQKQQ--EAELELEELKKKREERRKLleeeeQRRKQEEAERKLREE----EEKRRMKEE 321
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
639-881 |
1.34e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 639 SEIQTEPRETLEYKAALELEMWKEMQEDIFENQLKQKElahmqALAEEWKKRDRERE---SLVKKKVAEYTILEGKLQKT 715
Cdd:PRK03918 487 KVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKA-----EEYEKLKEKLIKLKgeiKSLKKELEKLEELKKKLAEL 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 716 LIDLEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKE--DCIHQVELERLKIKQLEEDKHRLQQQLNDAENK 793
Cdd:PRK03918 562 EKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLElkDAEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 794 YKILEKEFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSklhyKQQWGRALKEL-ARLKQREQ-ESQMARLK 871
Cdd:PRK03918 642 LEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKR----REEIKKTLEKLkEELEEREKaKKELEKLE 717
|
250
....*....|
gi 1769843751 872 KQQEELEQMR 881
Cdd:PRK03918 718 KALERVEELR 727
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
711-902 |
1.76e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 711 KLQKTLIDLEKREQQLASVESELQREKKELQSErqrnLQELQDSIRRAKEdcihqvelerlKIKQLEEDKHRLQQQLNDA 790
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEE----YNELQAELEALQA-----------EIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 791 ENKYKilekefQQFKDQQNNKpeiRLQSEINLLT--------LEKVELERKLESATKSKLhyKQQwgRALKELARLKQRE 862
Cdd:COG3883 85 REELG------ERARALYRSG---GSVSYLDVLLgsesfsdfLDRLSALSKIADADADLL--EEL--KADKAELEAKKAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1769843751 863 QESQMARLKKQQEELEQMRlrylaaEEKDTVKTERQELLD 902
Cdd:COG3883 152 LEAKLAELEALKAELEAAK------AELEAQQAEQEALLA 185
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
702-879 |
1.98e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 702 VAEYTILEGKLQKTLIDLEKREQQLasveseLQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEdkh 781
Cdd:PRK12704 19 VIGYFVRKKIAEAKIKEAEEEAKRI------LEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEK--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 782 RLQQqlndaenKYKILEKefqqfKDQQNNKPEIRLQSEINLLTLEKVELERKLESAtkSKLHYKQQwgRALKELARLKQR 861
Cdd:PRK12704 90 RLLQ-------KEENLDR-----KLELLEKREEELEKKEKELEQKQQELEKKEEEL--EELIEEQL--QELERISGLTAE 153
|
170
....*....|....*...
gi 1769843751 862 EQESQMarLKKQQEELEQ 879
Cdd:PRK12704 154 EAKEIL--LEKVEEEARH 169
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
654-918 |
2.15e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.58 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 654 ALELEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKlQKTLIDL----EKREQQLASV 729
Cdd:pfam15921 437 AMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS-ERTVSDLtaslQEKERAIEAT 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 730 ESELQRekkeLQSERQRNLQELQ------DSIRRAKEDCihqvelERLKIKQLEEDK--HRLQQQLndaENKYKILEKEF 801
Cdd:pfam15921 516 NAEITK----LRSRVDLKLQELQhlknegDHLRNVQTEC------EALKLQMAEKDKviEILRQQI---ENMTQLVGQHG 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 802 QQFKDQQNNKPEirLQSEINlltlekvelERKLEsatksklhykQQWGRALKELARLKQREQESQMARLkkqqeELEQMR 881
Cdd:pfam15921 583 RTAGAMQVEKAQ--LEKEIN---------DRRLE----------LQEFKILKDKKDAKIRELEARVSDL-----ELEKVK 636
|
250 260 270
....*....|....*....|....*....|....*..
gi 1769843751 882 LRYLAAEEKDTVKTERQELLDIRNELNSDIKKTNTVA 918
Cdd:pfam15921 637 LVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLS 673
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
722-889 |
2.49e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 722 REQQLASVESELQrEKKELQSERQRNLQELQdsirRAKEDcihqveLERLKIKQL--------EEDKHRLQQQLNDAENK 793
Cdd:PRK04863 784 REKRIEQLRAERE-ELAERYATLSFDVQKLQ----RLHQA------FSRFIGSHLavafeadpEAELRQLNRRRVELERA 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 794 YKILEKEFQQFKDQ-QNNKPEI----RLQSEINLL---TLEK--VELERKLESATKSKLhYKQQWGRALKELarlkqreq 863
Cdd:PRK04863 853 LADHESQEQQQRSQlEQAKEGLsalnRLLPRLNLLadeTLADrvEEIREQLDEAEEAKR-FVQQHGNALAQL-------- 923
|
170 180
....*....|....*....|....*.
gi 1769843751 864 ESQMARLKKQQEELEQMRLRYLAAEE 889
Cdd:PRK04863 924 EPIVSVLQSDPEQFEQLKQDYQQAQQ 949
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
637-903 |
2.51e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 637 CPSEIQTEPRETL--EYKAAL-----ELEMWKEMQEDIFENQ-------LKQKELAHMQALAEEWKKRDRERESL----V 698
Cdd:PRK03918 441 CGRELTEEHRKELleEYTAELkriekELKEIEEKERKLRKELrelekvlKKESELIKLKELAEQLKELEEKLKKYnleeL 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 699 KKKVAEYTILEGKL------QKTLIDLEKREQQLASVESELQREKKELQSErqrnLQELQDSIRRAKEDCIHQVElerLK 772
Cdd:PRK03918 521 EKKAEEYEKLKEKLiklkgeIKSLKKELEKLEELKKKLAELEKKLDELEEE----LAELLKELEELGFESVEELE---ER 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 773 IKQLEEdKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEirlqsEINLLTLEKVELERKLESATKSklhYKQQWGRAL 852
Cdd:PRK03918 594 LKELEP-FYNEYLELKDAEKELEREEKELKKLEEELDKAFE-----ELAETEKRLEELRKELEELEKK---YSEEEYEEL 664
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1769843751 853 KElarlKQREQESQMARLKKQQEELEQMR------LRYLaAEEKDTVKTERQELLDI 903
Cdd:PRK03918 665 RE----EYLELSRELAGLRAELEELEKRReeikktLEKL-KEELEEREKAKKELEKL 716
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
683-876 |
2.70e-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: 48.02 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 683 LAEEWKKRDRERESLVKKKVAEytiLEGKLQKtliDLEKREQQLASVESElQREKKELQSERQRNLQELQDSIRRAKEDC 762
Cdd:pfam15709 328 REQEKASRDRLRAERAEMRRLE---VERKRRE---QEEQRRLQQEQLERA-EKMREELELEQQRRFEEIRLRKQRLEEER 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 763 IHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQfKDQQNNKPEIRLQSEINLLTLEkvELERKLESATKSKL 842
Cdd:pfam15709 401 QRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQ-EEAERAEAEKQRQKELEMQLAE--EQKRLMEMAEEERL 477
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1769843751 843 HYKQQWGRAlKELARLK---QREQESQMARL-----KKQQEE 876
Cdd:pfam15709 478 EYQRQKQEA-EEKARLEaeeRRQKEEEAARLaleeaMKQAQE 518
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
652-834 |
4.27e-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: 46.98 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 652 KAALELEMwKEMQED-------IFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTI----LEGKLQKTLIDLE 720
Cdd:pfam15742 153 KKQLEERI-KEASENeaklkqqYQEEQQKRKLLDQNVNELQQQVRSLQDKEAQLEMTNSQQQLriqqQEAQLKQLENEKR 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 721 KREQQLASVE------SELQREKKELQSERQRNLQELQDSIR--------------RAKEDCIHQVELERLKIKQLEEDK 780
Cdd:pfam15742 232 KSDEHLKSNQelseklSSLQQEKEALQEELQQVLKQLDVHVRkynekhhhhkaklrRAKDRLVHEVEQRDERIKQLENEI 311
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1769843751 781 HRLQQQLNdaenkykiLEKEFQQFKDQQNNKpeirlqseinlLTLEKVELERKL 834
Cdd:pfam15742 312 GILQQQSE--------KEKAFQKQVTAQNEI-----------LLLEKRKLLEQL 346
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
681-906 |
4.34e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.17 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 681 QALAEEWKKRDRER-----ESLVKKKVAEYTILEGKL----QKTLIDLEKRE--QQLASVESELQREKKELQSERQRNLQ 749
Cdd:pfam02029 62 EAFLDRTAKREERRqkrlqEALERQKEFDPTIADEKEsvaeRKENNEEEENSswEKEEKRDSRLGRYKEEETEIREKEYQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 750 E--LQDSIRRAKEDCIHQvELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIRLQSEINLLTLEK 827
Cdd:pfam02029 142 EnkWSTEVRQAEEEGEEE-EDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLK 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 828 VELERKLES-----ATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEEleqmrlrylAAEEKDTVKTERQELLD 902
Cdd:pfam02029 221 VTTKRRQGGlsqsqEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQE---------AELELEELKKKREERRK 291
|
....
gi 1769843751 903 IRNE 906
Cdd:pfam02029 292 LLEE 295
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
711-915 |
5.40e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 711 KLQKTLIDLEKREQQLASVES---ELQREKKELQSERQRNLQELQDsirraKEDCIHQVELERLK-------IKQLEEDK 780
Cdd:TIGR04523 139 NIDKFLTEIKKKEKELEKLNNkynDLKKQKEELENELNLLEKEKLN-----IQKNIDKIKNKLLKlelllsnLKKKIQKN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 781 HRLQQQLNDAENKYKILEKEFQQfkdqqnnkpeirLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQ 860
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEK------------KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK 281
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1769843751 861 R--EQESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNELNSDIKKTN 915
Cdd:TIGR04523 282 KikELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIIS 338
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
723-915 |
5.53e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 723 EQQLASVESELQREKKELQSERQRN-LQELQDsirrakedcihQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEkef 801
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNgLVDLSE-----------EAKLLLQQLSELESQLAEARAELAEAEARLAALR--- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 802 QQFKDQQNNKPEIRLQSEINLLTLEKVELERklesatksklhykqqwgralkELARLKQR--EQESQMARLKKQQEELEQ 879
Cdd:COG3206 247 AQLGSGPDALPELLQSPVIQQLRAQLAELEA---------------------ELAELSARytPNHPDVIALRAQIAALRA 305
|
170 180 190
....*....|....*....|....*....|....*.
gi 1769843751 880 mRLRYLAAEEKDTVKTERQELLDIRNELNSDIKKTN 915
Cdd:COG3206 306 -QLQQEAQRILASLEAELEALQAREASLQAQLAQLE 340
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
642-841 |
5.81e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 642 QTEPRETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQAlaEEWKKRDRERESL--VKKKVAEYTILEGKLQKTLIDL 719
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--EELKKAEEEKKKVeqLKKKEAEEKKKAEELKKAEEEN 1659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 720 EKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEdcihQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEK 799
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE----AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1769843751 800 EFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSK 841
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
708-890 |
6.26e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 708 LEGKLQKTLIDLEKREQQLASVESELQREKKELQSERQRnLQELQDSIRRAKEdcihqvELERLKiKQLEEDKHRLQQQL 787
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-LEALQAEIDKLQA------EIAEAE-AEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 788 NDAenkYK----------ILE-KEFQQFKDQ--------QNNKPEIR-LQSEINLLTLEKVELERKLESATKSKLHYKQQ 847
Cdd:COG3883 93 RAL---YRsggsvsyldvLLGsESFSDFLDRlsalskiaDADADLLEeLKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1769843751 848 wgraLKELARlKQREQESQMARLKKQQEELEQMRLRYLAAEEK 890
Cdd:COG3883 170 ----KAELEA-QQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
644-907 |
6.38e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 644 EPRETLEYKAALELEmwKEMQEDIFENQLKQKelahmqalAEEWKKRDRE--RESLVKKKVAEYTILEGKLQKTLIDLEK 721
Cdd:PTZ00121 1294 EAKKAEEKKKADEAK--KKAEEAKKADEAKKK--------AEEAKKKADAakKKAEEAKKAAEAAKAEAEAAADEAEAAE 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 722 REQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERL--------KIKQLEEDKHRLQQQLNDAENK 793
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAaaakkkadEAKKKAEEKKKADEAKKKAEEA 1443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 794 YKI--LEKEFQQFKDQQNNKPEIRLQSEINLLTlEKVELERKLESATKSKLHYKQQwGRALKELARLKQREQESQMARLK 871
Cdd:PTZ00121 1444 KKAdeAKKKAEEAKKAEEAKKKAEEAKKADEAK-KKAEEAKKADEAKKKAEEAKKK-ADEAKKAAEAKKKADEAKKAEEA 1521
|
250 260 270
....*....|....*....|....*....|....*.
gi 1769843751 872 KQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNEL 907
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
665-870 |
7.34e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 665 EDIFENQLKQKelahmqaLAEEWKKRDRERESLVK------KKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKK 738
Cdd:COG4717 44 RAMLLERLEKE-------ADELFKPQGRKPELNLKelkeleEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 739 ELQS-ERQRNLQELQDSIRRAKE------DCIHQVELERLKIKQLEEDKHRLQQQLNDAENKykiLEKEFQQFkDQQNNK 811
Cdd:COG4717 117 ELEKlEKLLQLLPLYQELEALEAelaelpERLEELEERLEELRELEEELEELEAELAELQEE---LEELLEQL-SLATEE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1769843751 812 PEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARL 870
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
700-886 |
1.02e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 700 KKVAEYtilegKLQKTLIDLEKREQQLASVESELQREKKELQSERQRnLQELQDSIRRakedcihQVELERLKIKQLEED 779
Cdd:COG3206 196 AALEEF-----RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAE-AEARLAALRA-------QLGSGPDALPELLQS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 780 KH--RLQQQLNDAENKYKILEKEFqqfkdqQNNKPEIR-LQSEI-NLLTLEKVELERKLESATKSKLHYKQQWGRALKEL 855
Cdd:COG3206 263 PViqQLRAQLAELEAELAELSARY------TPNHPDVIaLRAQIaALRAQLQQEAQRILASLEAELEALQAREASLQAQL 336
|
170 180 190
....*....|....*....|....*....|....*.
gi 1769843751 856 ARLKQR-----EQESQMARLKKQQEELEQMRLRYLA 886
Cdd:COG3206 337 AQLEARlaelpELEAELRRLEREVEVARELYESLLQ 372
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
660-823 |
1.07e-04 |
|
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: 45.26 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 660 WKEMQEDIFE--NQLKQKELAHMQALAEEWKKrdrereslvKKKVAEyTILEGKLQKTLIDLEKREQQLASVESElqREK 737
Cdd:cd16269 147 YLEDREKLVEkyRQVPRKGVKAEEVLQEFLQS---------KEAEAE-AILQADQALTEKEKEIEAERAKAEAAE--QER 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 738 KELQSERQRNLQELQDSIRRakedciHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNkpeiRLQ 817
Cdd:cd16269 215 KLLEEQQRELEQKLEDQERS------YEEHLRQLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAE----LLQ 284
|
....*.
gi 1769843751 818 SEINLL 823
Cdd:cd16269 285 EEIRSL 290
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
743-909 |
1.08e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 743 ERQRNLQELQDSIRRAKEDC-IHQVELERLK---------IKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNnkp 812
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIaELEKALAELRkeleeleeeLEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA--- 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 813 eiRLQSEINLLTLEKVELERKLESATKsklhykqqwgrALKELARLKQrEQESQMARLkkqQEELEQMRLRYLAAEEKdt 892
Cdd:TIGR02168 751 --QLSKELTELEAEIEELEERLEEAEE-----------ELAEAEAEIE-ELEAQIEQL---KEELKALREALDELRAE-- 811
|
170
....*....|....*..
gi 1769843751 893 VKTERQELLDIRNELNS 909
Cdd:TIGR02168 812 LTLLNEEAANLRERLES 828
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
668-812 |
1.11e-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: 44.70 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 668 FENQLKQKELAHMQ-ALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESElQREKKELQSERQR 746
Cdd:pfam13904 57 YENWLAAKQRQRQKeLQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQQTKKREESHKQKAAE-SASKSLAKPERKV 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1769843751 747 nlqeLQDSIRRAKEDCIhQVELERLKIKQLEEDKHRLQQQLNDAENKyKILEKEFQQFKDQQNNKP 812
Cdd:pfam13904 136 ----SQEEAKEVLQEWE-RKKLEQQQRKREEEQREQLKKEEEEQERK-QLAEKAWQKWMKNVKNKP 195
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
670-921 |
1.20e-04 |
|
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: 45.94 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 670 NQLKQKELAHMQALAEEWKKRDRERESLVKKKvaeytileGKLQKTLIDLekREQQlasveSELQREKKELQSERQRNLQ 749
Cdd:pfam01576 179 SKLKNKHEAMISDLEERLKKEEKGRQELEKAK--------RKLEGESTDL--QEQI-----AELQAQIAELRAQLAKKEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 750 ELQDSIRRAKEDCIHQVELER------LKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFK-------DQQNNKPEIRL 816
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKkireleAQISELQEDLESERAARNKAEKQRRDLGEELEALKteledtlDTTAAQQELRS 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 817 QSEINLLTLEK------------------------VELERKLESAT-------KSKLHYKQQWGRALKELARLKQREQES 865
Cdd:pfam01576 324 KREQEVTELKKaleeetrsheaqlqemrqkhtqalEELTEQLEQAKrnkanleKAKQALESENAELQAELRTLQQAKQDS 403
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1769843751 866 QMARlKKQQEELEQMRLRYLAAEEkdtvktERQELLDIRNELNSDIKKTNTVATVA 921
Cdd:pfam01576 404 EHKR-KKLEGQLQELQARLSESER------QRAELAEKLSKLQSELESVSSLLNEA 452
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
713-889 |
1.21e-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: 44.31 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 713 QKTLIDLEKREQQLASVESELQREKKELQSERQRNLQElqdsirRAKEDcihqvelerlkikQLEEDKHRLqqqlndAEN 792
Cdd:pfam13904 41 ARKLEGLKLERQPLEAYENWLAAKQRQRQKELQAQKEE------REKEE-------------QEAELRKRL------AKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 793 KYK--ILEKEFQQFKDQQNNKPeirlQSEINLLTLEKVELERKlESATKSKLHYKQQWgraLKELARLKQREQESQMARL 870
Cdd:pfam13904 96 KYQewLQRKARQQTKKREESHK----QKAAESASKSLAKPERK-VSQEEAKEVLQEWE---RKKLEQQQRKREEEQREQL 167
|
170
....*....|....*....
gi 1769843751 871 KKQQEELEQMRLRYLAAEE 889
Cdd:pfam13904 168 KKEEEEQERKQLAEKAWQK 186
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
646-913 |
1.27e-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: 45.29 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 646 RETLEYKAALELEMWKEMQEDIF-----ENQLKQKELAHMQALAEEWKKRDRERESlvkkkvaeytilegKLQKTLIDLE 720
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEeeeekEEERKEERKRYRQELEEQIEEREQKRQE--------------EYEEKLQERE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 721 KREQQLASVESELQREKKELQSERQRNLQELQDSIR---RAKEDCIHQVELERLKIKQLEEDKHRLQQQLnDAENKYKIL 797
Cdd:pfam13868 102 QMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEeqaEWKELEKEEEREEDERILEYLKEKAEREEER-EAEREEIEE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 798 EKEFQQFKDQQNNKPEIRLQSEINLLTLEKVELErklesatksklhYKQQWGRALKELARLKQREQESQMARLKKQQEEL 877
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDELRAKLYQEE------------QERKERQKEREEAEKKARQRQELQQAREEQIELK 248
|
250 260 270
....*....|....*....|....*....|....*.
gi 1769843751 878 EQMRLRYLAAEEKDTVKTERQELLDIRNELNSDIKK 913
Cdd:pfam13868 249 ERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKR 284
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
639-800 |
1.59e-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: 45.83 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 639 SEIQTEPRETLEYKAALElEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQktliD 718
Cdd:TIGR02169 301 AEIASLERSIAEKERELE-DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE----E 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 719 LEKREQQLASVESELQREKKELQSER---QRNLQELQDSIRRA------------------------KEDCIHQVELERL 771
Cdd:TIGR02169 376 VDKEFAETRDELKDYREKLEKLKREInelKRELDRLQEELQRLseeladlnaaiagieakineleeeKEDKALEIKKQEW 455
|
170 180
....*....|....*....|....*....
gi 1769843751 772 KIKQLEEDKHRLQQQLNDAENKYKILEKE 800
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKE 484
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
643-877 |
1.77e-04 |
|
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: 45.55 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 643 TEPRETLEYKAAlELEMWKEMQEDiFENQLKQKELAH-------------MQALAEEWKKRDRERESLVKKKvaeytile 709
Cdd:pfam01576 1 TRQEEEMQAKEE-ELQKVKERQQK-AESELKELEKKHqqlceeknalqeqLQAETELCAEAEEMRARLAARK-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 710 GKLQKTLIDLEKREQQLASVESELQREKKELQSerqrNLQELQDSIRrAKEDCIHQVELERL----KIKQLEEDKHRLQQ 785
Cdd:pfam01576 71 QELEEILHELESRLEEEEERSQQLQNEKKKMQQ----HIQDLEEQLD-EEEAARQKLQLEKVtteaKIKKLEEDILLLED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 786 QLNDAENKYKILEKEFQQFKDQQNNKPE--IRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKqreq 863
Cdd:pfam01576 146 QNSKLSKERKLLEERISEFTSNLAEEEEkaKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQ---- 221
|
250
....*....|....
gi 1769843751 864 eSQMARLKKQQEEL 877
Cdd:pfam01576 222 -EQIAELQAQIAEL 234
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
602-901 |
1.83e-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: 45.34 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 602 LEDYGLVKMREIFISDSSQGVSAVQQKPSSLPPAPCPSEIQTEPretlEYKAALELEMwKEMQEDIFENQLKQKELAHMQ 681
Cdd:TIGR00618 175 LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYH----ERKQVLEKEL-KHLREALQQTQQSHAYLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 682 ALAEEWKKRDRERESLVKKkVAEYTILEGKLQKTLIDLEKR----------------EQQLASVESELQREKKELQSERQ 745
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRAR-IEELRAQEAVLEETQERINRArkaaplaahikavtqiEQQAQRIHTELQSKMRSRAKLLM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 746 R---------NLQELQDSIRRAKEDCIH----------------QVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKE 800
Cdd:TIGR00618 329 KraahvkqqsSIEEQRRLLQTLHSQEIHirdahevatsireiscQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 801 fqqfkdqqNNKPEIRLQSEiNLLTLEKVELeRKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEELEQM 880
Cdd:TIGR00618 409 --------QATIDTRTSAF-RDLQGQLAHA-KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK 478
|
330 340
....*....|....*....|.
gi 1769843751 881 RLRYLAAEEKDTVKTERQELL 901
Cdd:TIGR00618 479 EQIHLQETRKKAVVLARLLEL 499
|
|
| Granin |
pfam01271 |
Granin (chromogranin or secretogranin); |
639-889 |
1.87e-04 |
|
Granin (chromogranin or secretogranin);
Pssm-ID: 279595 [Multi-domain] Cd Length: 584 Bit Score: 45.02 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 639 SEIQTEPRETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQ-ALAEEWKKRDRERESLVKKKVAEYTilegklQKTLI 717
Cdd:pfam01271 98 NEPGGHSRENQPYALQVEKEFKTDHSDDYETQQWEEEKLKHMRfPLRYEENSEEKHSEREGELSEVFEN------PRSQA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 718 DLEKREQQLASVESElQREKKELQSERQRNLQELQDSIRRAKEdciHQVELERLKIKQlEEDKHRLQQQLNDAENKYKIL 797
Cdd:pfam01271 172 TLKKVFEEVSRLDTP-SKQKREKSDEREKSSQESGEDTYRQEN---IPQEDQVGPEDQ-EPSEEGEEDATQEEVKRSRPR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 798 EKEFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQ--QE 875
Cdd:pfam01271 247 THHGRSLPDESSRGGQLGLEEEASEEEEEYGEESRGLSAVQTYLLRLVNARGRGRSEKRAERERSEESEEEELKRAspYE 326
|
250
....*....|....
gi 1769843751 876 ELEQMRLRYLAAEE 889
Cdd:pfam01271 327 ELEITANLQIPPSE 340
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
692-911 |
2.04e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.42 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 692 RERESLVKKKVAEYTILEGK--LQKTLIDLEKRE-----QQLASVESELQREKKELqsERQRNLQELQDSIRRAKEDCIH 764
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLGLapGRQSIIDLKEKEipelrNKLQKVNRDIQRLKNDI--EEQETLLGTIMPEEESAKVCLT 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 765 QVELERLKIKQLEEDKHRLQQQLN-----DAENKYKILEKEFQQFKD----------------QQNNKPEIRLQSEINLL 823
Cdd:TIGR00606 790 DVTIMERFQMELKDVERKIAQQAAklqgsDLDRTVQQVNQEKQEKQHeldtvvskielnrkliQDQQEQIQHLKSKTNEL 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 824 TLEKVEL------ERKLESATKSKLHYKQQWGRALKElarlkQREQESQMARLKKQqeelEQMRLRYLAAEEKDTVKTER 897
Cdd:TIGR00606 870 KSEKLQIgtnlqrRQQFEEQLVELSTEVQSLIREIKD-----AKEQDSPLETFLEK----DQQEKEELISSKETSNKKAQ 940
|
250
....*....|....
gi 1769843751 898 QELLDIRNELNSDI 911
Cdd:TIGR00606 941 DKVNDIKEKVKNIH 954
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
783-913 |
2.06e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 783 LQQQLNDAENKYKILEKEFQQFKdQQNNkpEIRLQSEINLLTLEKVELERKLESAT------KSKLHY-KQQWGRALKEL 855
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFR-QKNG--LVDLSEEAKLLLQQLSELESQLAEARaelaeaEARLAAlRAQLGSGPDAL 256
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1769843751 856 ARLKQREQESQM-ARLKKQQEELEQMRLRYLaaEEKDTVKTERQELLDIRNELNSDIKK 913
Cdd:COG3206 257 PELLQSPVIQQLrAQLAELEAELAELSARYT--PNHPDVIALRAQIAALRAQLQQEAQR 313
|
|
| C2 |
pfam00168 |
C2 domain; |
9-114 |
2.15e-04 |
|
C2 domain;
Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 41.54 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 9 LIVVSILEGRHFPKRPKHMLV---VEAKFDGEQ--LATDPVDHTDQPEFATELAWEIdrkalhqHRLQRTPIKLQCFALD 83
Cdd:pfam00168 2 RLTVTVIEAKNLPPKDGNGTSdpyVKVYLLDGKqkKKTKVVKNTLNPVWNETFTFSV-------PDPENAVLEIEVYDYD 74
|
90 100 110
....*....|....*....|....*....|.
gi 1769843751 84 pVTSAKETIGYIVLDLRTAQETKQAPKWYQL 114
Cdd:pfam00168 75 -RFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
719-908 |
2.89e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.46 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 719 LEKREQQLASVESELQREK---KELQSERQRNLQELQDSIRRAKEDCIH------QVELERLKiKQLEEDKHRLQQ-QLN 788
Cdd:pfam06160 181 LEKLEEETDALEELMEDIPplyEELKTELPDQLEELKEGYREMEEEGYAlehlnvDKEIQQLE-EQLEENLALLENlELD 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 789 DAENK-----------YKILEKEFQQFKDQQNNKPEIR------------LQSEINLL---------TLEKV-ELERKLE 835
Cdd:pfam06160 260 EAEEAleeieeridqlYDLLEKEVDAKKYVEKNLPEIEdylehaeeqnkeLKEELERVqqsytlnenELERVrGLEKQLE 339
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1769843751 836 SATKSKLHYKQQWGRalKELA----RLKQREQESQMARLKKQQEELEQMrLRYLAAEEKDTvkteRQELLDIRNELN 908
Cdd:pfam06160 340 ELEKRYDEIVERLEE--KEVAyselQEELEEILEQLEEIEEEQEEFKES-LQSLRKDELEA----REKLDEFKLELR 409
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
674-889 |
2.94e-04 |
|
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: 44.26 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 674 QKELAHMQALAEEWKKRDRERESLvkkkvaEYTILEGKLQKTLIDLEKRE---QQLASVESELQREKKELQSERQRNLQE 750
Cdd:pfam15558 37 LRRRDQKRQETLERERRLLLQQSQ------EQWQAEKEQRKARLGREERRradRREKQVIEKESRWREQAEDQENQRQEK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 751 LQDSIRRAKEDCIHQVelERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIRLQSEINLLTLeKVEL 830
Cdd:pfam15558 111 LERARQEAEQRKQCQE--QRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQAR-KVLV 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1769843751 831 ERK-----------LE-SATKSKLHYKQQWGRALKEL-ARLKQREQESQMARLK-KQQEELEQMRLRYLAAEE 889
Cdd:pfam15558 188 DCQakaeellrrlsLEqSLQRSQENYEQLVEERHRELrEKAQKEEEQFQRAKWRaEEKEEERQEHKEALAELA 260
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
702-916 |
3.02e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 702 VAEYTILEGKLQKTLIDLEKREQQLA---SVESELQREKKELQSERQ-------------RNLQELQDSIRRAKEDC--- 762
Cdd:PRK01156 182 ISNIDYLEEKLKSSNLELENIKKQIAddeKSHSITLKEIERLSIEYNnamddynnlksalNELSSLEDMKNRYESEIkta 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 763 ---IHQVELERLKIKQLEEdkhRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEI--RLQSEINlltlEKVELERKLESA 837
Cdd:PRK01156 262 esdLSMELEKNNYYKELEE---RHMKIINDPVYKNRNYINDYFKYKNDIENKKQIlsNIDAEIN----KYHAIIKKLSVL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 838 TKSKLHY---KQQWGRALKELARLKQREQESQMA-------RLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNEL 907
Cdd:PRK01156 335 QKDYNDYikkKSRYDDLNNQILELEGYEMDYNSYlksieslKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEI 414
|
....*....
gi 1769843751 908 NSDIKKTNT 916
Cdd:PRK01156 415 NVKLQDISS 423
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
712-913 |
3.09e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 712 LQKTLIDLEKREQQLASVESELQRekKELQSERQrnLQELQDSirrakedcihQVELERLKIKQLEEDKHRLQQQLNDae 791
Cdd:PRK11281 189 LRPSQRVLLQAEQALLNAQNDLQR--KSLEGNTQ--LQDLLQK----------QRDYLTARIQRLEHQLQLLQEAINS-- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 792 nKYKIL-EKEFQQFKDQQNNK-----PEIRLQSEINLltlekvELERKLESAT-------------KSKLHYKQQWGRAL 852
Cdd:PRK11281 253 -KRLTLsEKTVQEAQSQDEAAriqanPLVAQELEINL------QLSQRLLKATeklntltqqnlrvKNWLDRLTQSERNI 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 853 KE----------LARLKQREQES------------QMARLKKQQEELEQMR-------------LRYLAAEEKDTVKTER 897
Cdd:PRK11281 326 KEqisvlkgsllLSRILYQQQQAlpsadliegladRIADLRLEQFEINQQRdalfqpdayidklEAGHKSEVTDEVRDAL 405
|
250
....*....|....*.
gi 1769843751 898 QELLDIRNELNSDIKK 913
Cdd:PRK11281 406 LQLLDERRELLDQLNK 421
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
719-920 |
3.28e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.31 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 719 LEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEdkhRLQQQLNDAENKYKile 798
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEE---RLVQKEEQLDARAE--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 799 kefqqfkdqqnnkpeirlqsEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEElE 878
Cdd:PRK12705 99 --------------------KLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELE-E 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1769843751 879 QMRLRYLAAEEKDTVKTERQELLDIRNELN---SDIKKTNTVATV 920
Cdd:PRK12705 158 EKAQRVKKIEEEADLEAERKAQNILAQAMQriaSETASDLSVSVV 202
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
661-917 |
3.43e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 661 KEMQEDIFENQLK--QKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEgKLQKTLIDLEKRE-QQLASVESELQREK 737
Cdd:TIGR04523 31 QDTEEKQLEKKLKtiKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILE-QQIKDLNDKLKKNkDKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 738 KELQSERQrNLQELQDSIRRAKEDcihQVELERLKIKQLEEDKhRLQQQLNDAENKYKILEKEFQQFKDQQN--NKPEIR 815
Cdd:TIGR04523 110 SEIKNDKE-QKNKLEVELNKLEKQ---KKENKKNIDKFLTEIK-KKEKELEKLNNKYNDLKKQKEELENELNllEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 816 LQSEINLLTLEKVELERKLesatkSKLHYKQQwgralkelarlKQREQESQMARLKKQQEELeqmrlrylaaeeKDTVKT 895
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLL-----SNLKKKIQ-----------KNKSLESQISELKKQNNQL------------KDNIEK 236
|
250 260
....*....|....*....|..
gi 1769843751 896 ERQELLDIRNELNSDIKKTNTV 917
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQL 258
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
656-902 |
3.69e-04 |
|
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: 44.40 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 656 ELEMWKEMQEDIFENQLKQKEL--------AHMQ-ALAEEWKKRDRERESLVKKKVAEYTILEGKLQKT---LIDLEKRE 723
Cdd:pfam01576 300 ELEALKTELEDTLDTTAAQQELrskreqevTELKkALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAkrnKANLEKAK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 724 QQLASVESELQREKKELQ-----SERQRNLQE--LQDSIRRAKEDCIHQVEL-ERLKIKQLEEDKhrLQQQLNDAENKYK 795
Cdd:pfam01576 380 QALESENAELQAELRTLQqakqdSEHKRKKLEgqLQELQARLSESERQRAELaEKLSKLQSELES--VSSLLNEAEGKNI 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 796 ILEKEF----QQFKD-----QQNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQ 866
Cdd:pfam01576 458 KLSKDVssleSQLQDtqellQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA 537
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1769843751 867 MA------RLKKQQEELEQMRLRY----LAAEEKDTVKTERQELLD 902
Cdd:pfam01576 538 GTlealeeGKKRLQRELEALTQQLeekaAAYDKLEKTKNRLQQELD 583
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
655-879 |
3.75e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.47 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 655 LELEMW--KEMQEDI-----FENQLKQKELAHMQALAEEWKKRDRERESLVKKK---VAEYTILEGK---------LQKT 715
Cdd:smart00787 65 LELYQFscKELKKYIsegrdLFKEIEEETLINNPPLFKEYFSASPDVKLLMDKQfqlVKTFARLEAKkmwyewrmkLLEG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 716 LIDlekreqQLASVESELQREKKELQSERQRnLQELQDSIRRAKEDCIHQVELERlkikQLEEDKHRLQQ-QLNDAENKY 794
Cdd:smart00787 145 LKE------GLDENLEGLKEDYKLLMKELEL-LNSIKPKLRDRKDALEEELRQLK----QLEDELEDCDPtELDRAKEKL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 795 KILEKEFQQFKDQQNNkpeirlqseinlLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREqESQMARLKKQQ 874
Cdd:smart00787 214 KKLLQEIMIKVKKLEE------------LEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFT-FKEIEKLKEQL 280
|
....*
gi 1769843751 875 EELEQ 879
Cdd:smart00787 281 KLLQS 285
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
674-907 |
4.59e-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: 44.19 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 674 QKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQktlidLEKREQQLASVESELQREKKELQSERQRNLQELQD 753
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN-----ITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 754 SIRRAKEDCIHQVELErlkikQLEEDKHRLQQQLNDAENKYKILE-KEFQQFKDQQNNKPEIRLQSEINLLTLEKVELER 832
Cdd:TIGR00618 627 LQDVRLHLQQCSQELA-----LKLTALHALQLTLTQERVREHALSiRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 833 K-------LESATKSKLHYKQQWGRALKELARLKQRE----------QESQMARLKKQQEELEQMRLRYLAAEEKDTVKT 895
Cdd:TIGR00618 702 CqtllrelETHIEEYDREFNEIENASSSLGSDLAAREdalnqslkelMHQARTVLKARTEAHFNNNEEVTAALQTGAELS 781
|
250
....*....|..
gi 1769843751 896 ERQELLDIRNEL 907
Cdd:TIGR00618 782 HLAAEIQFFNRL 793
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
770-914 |
5.10e-04 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 42.20 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 770 RLKIKQLEEDKHRLQQQLNDAENKYKIL-------EKEFQQFKDQQNNKPEI--RLQSEINLLTLEKVELERKLESATKS 840
Cdd:pfam15619 10 LHKIKELQNELAELQSKLEELRKENRLLkrlqkrqEKALGKYEGTESELPQLiaRHNEEVRVLRERLRRLQEKERDLERK 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1769843751 841 KLHYKQQWGRALKELARLKQREQESQMARLKKQQEELEQMRLRYLAAEEKdTVKTERQ-ELLD--IRNELNSDIKKT 914
Cdd:pfam15619 90 LKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEK-IQDLERKlELENksFRRQLAAEKKKH 165
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
639-876 |
5.63e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 639 SEIQTEPRETLEyKAALELEMWKEMQEDIFEN------QLKQKELAHMQALAEEWK----------KRDRERESLvkkKV 702
Cdd:pfam15921 137 SQSQEDLRNQLQ-NTVHELEAAKCLKEDMLEDsntqieQLRKMMLSHEGVLQEIRSilvdfeeasgKKIYEHDSM---ST 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 703 AEYTILEGKLQKTLIDLEKR----EQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDciHQVELERLKIK---- 774
Cdd:pfam15921 213 MHFRSLGSAISKILRELDTEisylKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISE--HEVEITGLTEKassa 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 775 ---------QLE--EDKHRLQ-----QQLNDAENKYKILEKEFQQFKDQQNNKPEiRLQSEINLLTLEKVE--LERKLES 836
Cdd:pfam15921 291 rsqansiqsQLEiiQEQARNQnsmymRQLSDLESTVSQLRSELREAKRMYEDKIE-ELEKQLVLANSELTEarTERDQFS 369
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1769843751 837 ATKSKLHYKQQwgralKELARLKQREQEsqmARLKKQQEE 876
Cdd:pfam15921 370 QESGNLDDQLQ-----KLLADLHKREKE---LSLEKEQNK 401
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
684-899 |
5.65e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 684 AEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKEL-QSERQRNLQELQDSIRRAK--E 760
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkKAEEKKKADEAKKKAEEAKkaD 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 761 DCIHQVELERLKI----KQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIRLQSEinlLTLEKVELERKLES 836
Cdd:PTZ00121 1319 EAKKKAEEAKKKAdaakKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD---AAKKKAEEKKKADE 1395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1769843751 837 ATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEELEQmrlrylAAEEK---DTVKTERQE 899
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK------KAEEAkkaDEAKKKAEE 1455
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
640-910 |
7.19e-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: 43.42 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 640 EIQTEPRETLEYKAALELEMWKEMQEDIFENQLKQkELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDL 719
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE-DIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQ 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 720 EKR------EQQLASVESELQREKKELQSERQRnlqelqDSIRRAKEDcihqvELERLKIKQLEEDK--HRLQQQLNDAE 791
Cdd:TIGR00618 629 DVRlhlqqcSQELALKLTALHALQLTLTQERVR------EHALSIRVL-----PKELLASRQLALQKmqSEKEQLTYWKE 697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 792 NKYKILEKEFQQFKDQQNNKPEIRLQSeiNLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLK 871
Cdd:TIGR00618 698 MLAQCQTLLRELETHIEEYDREFNEIE--NASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQ 775
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1769843751 872 KQQEELEQMRLRYLAAEEKDTVKTERQELL-DIRNELNSD 910
Cdd:TIGR00618 776 TGAELSHLAAEIQFFNRLREEDTHLLKTLEaEIGQEIPSD 815
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
673-882 |
7.63e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 673 KQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQseRQRNLQELQ 752
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIA 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 753 DSIRRAKED--------CIHQVELERLKiKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIRLQSEINLLT 824
Cdd:COG4717 374 ALLAEAGVEdeeelraaLEQAEEYQELK-EELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELR 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1769843751 825 LEKVELERKLESATKSKL--HYKQQWGRALKELARLKQREQESQMAR--LKKQQEELEQMRL 882
Cdd:COG4717 453 EELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALelLEEAREEYREERL 514
|
|
| BRE1 |
pfam08647 |
BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a ... |
674-791 |
8.63e-04 |
|
BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a transcriptional activator through direct activator interactions.
Pssm-ID: 462547 [Multi-domain] Cd Length: 95 Bit Score: 39.49 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 674 QKELAHMQAlaeEWKKRDrereSLVKKKVAEYTILEGKLQKTLIDLEKREQQLAsvesELQREKKELQSERqRNLQelqd 753
Cdd:pfam08647 2 QTELVKLEQ---AFEELS----EQLDKKVKDLTILEEKKLRLEAEKAKADQKYF----AAMRSKDALENEN-KKLN---- 65
|
90 100 110
....*....|....*....|....*....|....*...
gi 1769843751 754 sirrakedciHQVELERLKIKQLEEDKHRLQQQLNDAE 791
Cdd:pfam08647 66 ----------TLLSKSSELIEQLKETEKEFVRKLKNLE 93
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
748-907 |
8.87e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.90 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 748 LQELQDSIRRAKEDcihqveLERLKIKQLEEDKHRLQQQLNDAenkYKILEKEFQQFKDQQNNKPEIR------------ 815
Cdd:PRK04778 258 IQDLKEQIDENLAL------LEELDLDEAEEKNEEIQERIDQL---YDILEREVKARKYVEKNSDTLPdflehakeqnke 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 816 LQSEINLLT---------LEKV-ELERKLESATKSKLHYKQQW--GRALKELARLKQREQESQMARLKKQQEELEQMrLR 883
Cdd:PRK04778 329 LKEEIDRVKqsytlneseLESVrQLEKQLESLEKQYDEITERIaeQEIAYSELQEELEEILKQLEEIEKEQEKLSEM-LQ 407
|
170 180
....*....|....*....|....*..
gi 1769843751 884 YLAAEE---KDTVKTERQELLDIRNEL 907
Cdd:PRK04778 408 GLRKDEleaREKLERYRNKLHEIKRYL 434
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
732-916 |
8.95e-04 |
|
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: 42.96 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 732 ELQREKKELQSER---QRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILE-------KEF 801
Cdd:pfam07888 38 ECLQERAELLQAQeaaNRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSasseelsEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 802 QQFKDQQ-NNKPEIR-LQSEINLLTLEKVELERKLESATKsklhykqqwgRALKELARLKQREQESQMARLKKQQEELEQ 879
Cdd:pfam07888 118 DALLAQRaAHEARIReLEEDIKTLTQRVLERETELERMKE----------RAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 1769843751 880 MRLRYLAAEEKDTVKTERQELLDIRNELNSDIKKTNT 916
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTT 224
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
638-797 |
9.25e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.20 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 638 PSEIqtePRETLEYKAALELEMWKEMQED-------IFENQLKQKELAHMQALAEEWKKR-----DRERESLVKKKVAEY 705
Cdd:pfam07111 232 PPEV---HSQTWELERQELLDTMQHLQEDradlqatVELLQVRVQSLTHMLALQEEELTRkiqpsDSLEPEFPKKCRSLL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 706 TILEGKLQKTLIDLEKREQQLASVESELQREKKELQSERQRNLQElQDSIRRAKEDCIHQVELERLKIKQL-------EE 778
Cdd:pfam07111 309 NRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQE-QAILQRALQDKAAEVEVERMSAKGLqmelsraQE 387
|
170
....*....|....*....
gi 1769843751 779 DKHRLQQQLNDAENKYKIL 797
Cdd:pfam07111 388 ARRRQQQQTASAEEQLKFV 406
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
674-913 |
9.37e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 674 QKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQktliDLEKREQQLASVESELQREKKELQSERQRNLQELQD 753
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVS----DLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKT 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 754 SiRRAKEDCIHQVELE----RLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFK--DQQNNKPEIRLQS-------EI 820
Cdd:pfam15921 665 S-RNELNSLSEDYEVLkrnfRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsDGHAMKVAMGMQKqitakrgQI 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 821 NLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQE---------SQMARLKKQ----QEELEQMRLRYlaA 887
Cdd:pfam15921 744 DALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKmagelevlrSQERRLKEKvanmEVALDKASLQF--A 821
|
250 260
....*....|....*....|....*.
gi 1769843751 888 EEKDTVKTERQELLDIRNELNSDIKK 913
Cdd:pfam15921 822 ECQDIIQRQEQESVRLKLQHTLDVKE 847
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
641-916 |
1.03e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 641 IQTEPRETLEYKAALE-LEMWKEMQEDIfENQLKQKElAHMQALAEEWKKRDRERESLVK--KKVAEYTILEGKLQKTLI 717
Cdd:TIGR00606 195 RQTQGQKVQEHQMELKyLKQYKEKACEI-RDQITSKE-AQLESSREIVKSYENELDPLKNrlKEIEHNLSKIMKLDNEIK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 718 DLEKREQQLASVESEL----------------------QREKKELQSERQRNLQELQDSIRRAKEDCIHQVELE-RLKIK 774
Cdd:TIGR00606 273 ALKSRKKQMEKDNSELelkmekvfqgtdeqlndlyhnhQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLvEQGRL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 775 QLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIRlqseiNLLTLEKVELERKLESATK------SKLHYKQQW 848
Cdd:TIGR00606 353 QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIK-----NFHTLVIERQEDEAKTAAQlcadlqSKERLKQEQ 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 849 GRALKELARLKQREQESQMARLKKQQEELEQMR--LRYLAAEEKDTVKTErQELLDIRNELNSDIKKTNT 916
Cdd:TIGR00606 428 ADEIRDEKKGLGRTIELKKEILEKKQEELKFVIkeLQQLEGSSDRILELD-QELRKAERELSKAEKNSLT 496
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
730-858 |
1.32e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 730 ESELQREKKELQSERQRNLQELQDSIRRAKEdcihqveLERlKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQN 809
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEEIRR-------LEE-QVERLEAEVEELEAELEEKDERIERLERELSEARSEER 458
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1769843751 810 NkpEIRLQSEINLLTLEKVELERKLESA--TKSKLHYKQQwgrALKELARL 858
Cdd:COG2433 459 R--EIRKDREISRLDREIERLERELEEEreRIEELKRKLE---RLKELWKL 504
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
684-908 |
1.58e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 684 AEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESEL------------QREK-----KELQSERQR 746
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerfgdapvDLGNaedflEELREERDE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 747 ----------NLQELQDSIRRAK------------------------EDCIHQVELERLKIKQLEEDKHRLQQQLNDAEn 792
Cdd:PRK02224 424 lrereaeleaTLRTARERVEEAEalleagkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAE- 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 793 KYKILEKEFQQFKDQQNNKPEIRLQSEINL---------LTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQ 863
Cdd:PRK02224 503 DLVEAEDRIERLEERREDLEELIAERRETIeekreraeeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA 582
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1769843751 864 EsqmarLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNELN 908
Cdd:PRK02224 583 E-----LKERIESLERIRTLLAAIADAEDEIERLREKREALAELN 622
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
711-906 |
1.68e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.20 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 711 KLQKTL-IDLEKREQQLASVESELQREKKELQ------SERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHR- 782
Cdd:pfam15964 371 RLEKELaSQQEKRAQEKEALRKEMKKEREELGatmlalSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKv 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 783 ---LQQQLNDAENKYKILEKEFQQFKDQQNNKPEIRLQsEINLLTLEKVELERKLESAtksklhyKQQWGRALKELAR-- 857
Cdd:pfam15964 451 cgeMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQ-EIEKLGLELSESKQRLEQA-------QQDAARAREECLKlt 522
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1769843751 858 --LKQREQESQMARLKK---QQEELEQMRLRYLAAEEKDTVKTERQELLDIRNE 906
Cdd:pfam15964 523 elLGESEHQLHLTRLEKesiQQSFSNEAKAQALQAQQREQELTQKMQQMEAQHD 576
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
708-904 |
1.71e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 708 LEGKLQKTLIDLEKREQQLASVESELQREKKELQSERQRNLQEL----QDSIRRAKEdcihqvELERLkIKQLeedkhRL 783
Cdd:PRK00409 528 LERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaQQAIKEAKK------EADEI-IKEL-----RQ 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 784 QQQLNDAENKYKILEKEFQQFKDQQNNKPEIrlqseinllTLEKVELERKLESATKSKLHYKQQWGRALKELAR------ 857
Cdd:PRK00409 596 LQKGGYASVKAHELIEARKRLNKANEKKEKK---------KKKQKEKQEELKVGDEVKYLSLGQKGEVLSIPDDkeaivq 666
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1769843751 858 ---LKQREQESQMARLKKQQEELEQMrlrylAAEEKDTVKTERQElLDIR 904
Cdd:PRK00409 667 agiMKMKVPLSDLEKIQKPKKKKKKK-----PKTVKPKPRTVSLE-LDLR 710
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
646-842 |
1.73e-03 |
|
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: 41.67 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 646 RETLEYKAALELEMWKEMQEDIFENQLKQKELAhmQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLI------DL 719
Cdd:COG4942 57 LAALERRIAALARRIRALEQELAALEAELAELE--KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLspedflDA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 720 EKREQQLASVESELQREKKELQSERQRnLQELQDSIRRAKEdcihqvELERLKiKQLEEDKHRLQQQLNDAENKYKILEK 799
Cdd:COG4942 135 VRRLQYLKYLAPARREQAEELRADLAE-LAALRAELEAERA------ELEALL-AELEEERAALEALKAERQKLLARLEK 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1769843751 800 EFQQFKDQ--QNNKPEIRLQSEINLLTLEKVELERKLESATKSKL 842
Cdd:COG4942 207 ELAELAAElaELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
685-790 |
2.58e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.27 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 685 EEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLAsvesELQREKKELQSERQRnLQELQDSIRRAKEDciH 764
Cdd:pfam13851 36 AELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLE----NYEKDKQSLKNLKAR-LKVLEKELKDLKWE--H 108
|
90 100
....*....|....*....|....*.
gi 1769843751 765 QVELERLkiKQLEEDKHRLQQQLNDA 790
Cdd:pfam13851 109 EVLEQRF--EKVERERDELYDKFEAA 132
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
699-925 |
2.75e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 699 KKKVAEYTILEGKLQKTLIDLEKREQQ----LASVESELQREKKELQSERQRNLQELQDSIRRAKEdcihqveleRLKIK 774
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEellaALGLPPDLSPEELLELLDRIEELQELLREAEELEE---------ELQLE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 775 QLEEDKHRLQQQLN-DAENKYKILEKEFQQFKDQQNNKPEIRLQseinlLTLEKVELERKLESATKSKLhyKQQWGRALK 853
Cdd:COG4717 367 ELEQEIAALLAEAGvEDEEELRAALEQAEEYQELKEELEELEEQ-----LEELLGELEELLEALDEEEL--EEELEELEE 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1769843751 854 ELARLkQREQESQMARLKKQQEELEQMrlrylaaEEKDTVKTERQELLDIRNELNSDIKKTNTVATVAFVLD 925
Cdd:COG4717 440 ELEEL-EEELEELREELAELEAELEQL-------EEDGELAELLQELEELKAELRELAEEWAALKLALELLE 503
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
678-899 |
3.20e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 678 AHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESE---LQREKKELQSERQRNLQELQDS 754
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEidkLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 755 IRRAKEDCIHQVELER-LKIKQLEEDKHRLQ--QQLNDAENkyKILEkEFQQFKDQQNNKpEIRLQSEINLLTLEKVELE 831
Cdd:COG3883 92 ARALYRSGGSVSYLDVlLGSESFSDFLDRLSalSKIADADA--DLLE-ELKADKAELEAK-KAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769843751 832 RKLESATKSKlhyKQQwgRALKELARLKQREQESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQE 899
Cdd:COG3883 168 AAKAELEAQQ---AEQ--EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
680-766 |
3.32e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 39.43 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 680 MQALAEEWKKRDRERESLVKKKVAEYTILEGKLQK-----TLIDLEKREQQLASVESELQREKKELQSERQRNLQELQDS 754
Cdd:COG2825 41 GKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKeaatlSEEERQKKERELQKKQQELQRKQQEAQQDLQKRQQELLQP 120
|
90
....*....|..
gi 1769843751 755 IRRAKEDCIHQV 766
Cdd:COG2825 121 ILEKIQKAIKEV 132
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
681-923 |
3.70e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 681 QALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVEselQREKKELQSERQRNLQELQDSIRRAKE 760
Cdd:PRK01156 493 KDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELK---DKHDKYEEIKNRYKSLKLEDLDSKRTS 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 761 DCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKdQQNNKPEIRLQSEINLLTLEKVELE---RKLESA 837
Cdd:PRK01156 570 WLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDK-SYIDKSIREIENEANNLNNKYNEIQenkILIEKL 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 838 TKSKLHYKqqwgralKELARLKQRE--QESQMARLKKQQEELEQMRLRYLA-----AEEKDTVKTERQ---ELLDIRNEL 907
Cdd:PRK01156 649 RGKIDNYK-------KQIAEIDSIIpdLKEITSRINDIEDNLKKSRKALDDakanrARLESTIEILRTrinELSDRINDI 721
|
250
....*....|....*..
gi 1769843751 908 NSDIKKTNTV-ATVAFV 923
Cdd:PRK01156 722 NETLESMKKIkKAIGDL 738
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
644-880 |
4.00e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.98 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 644 EPRETLEYKAAL------ELEMWKEMQEDIFENQLKQKELaHMQALAEEWK-KRDRERESL------VKKKVAEYTILEG 710
Cdd:pfam12128 251 NTLESAELRLSHlhfgykSDETLIASRQEERQETSAELNQ-LLRTLDDQWKeKRDELNGELsaadaaVAKDRSELEALED 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 711 KLQKTL-IDLEKREQ---QLASVESEL--QREKKELQSERQRNLQELQDSiRRAKEDCIHQVELERLKiKQLEEDKHRLQ 784
Cdd:pfam12128 330 QHGAFLdADIETAAAdqeQLPSWQSELenLEERLKALTGKHQDVTAKYNR-RRSKIKEQNNRDIAGIK-DKLAKIREARD 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 785 QQLNDAENKYKILEKEFQQFKDQQNNK-------------------------PEIRLQSEINLLTLEKVEleRKLESATK 839
Cdd:pfam12128 408 RQLAVAEDDLQALESELREQLEAGKLEfneeeyrlksrlgelklrlnqatatPELLLQLENFDERIERAR--EEQEAANA 485
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1769843751 840 SKLhykqqwgRALKELARLKQREQESQMA------RLKKQQ---EELEQM 880
Cdd:pfam12128 486 EVE-------RLQSELRQARKRRDQASEAlrqasrRLEERQsalDELELQ 528
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
680-832 |
4.17e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.56 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 680 MQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQSERQRNlQELQDSIRRAk 759
Cdd:pfam15905 154 MSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSET-EKLLEYITEL- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 760 EDCIHQVELERLKIKQLEED------------------KHRLQQQLNDAENKYKILEKEFQQfKDQQNNKPEIRLQSEIN 821
Cdd:pfam15905 232 SCVSEQVEKYKLDIAQLEELlkekndeieslkqsleekEQELSKQIKDLNEKCKLLESEKEE-LLREYEEKEQTLNAELE 310
|
170
....*....|.
gi 1769843751 822 LLTlEKVELER 832
Cdd:pfam15905 311 ELK-EKLTLEE 320
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
661-914 |
4.27e-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: 41.11 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 661 KEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILegKLQKTLIDLEKREQQLASVESELQREKKEL 740
Cdd:TIGR00618 335 KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH--TLQQQKTTLTQKLQSLCKELDILQREQATI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 741 QSERQRNlQELQDSIRRAKEDCihQVELERLKIKQLEEDKHRLQQQLNDA---ENKYKILEKEFQQFKDQQNNKPEIRLQ 817
Cdd:TIGR00618 413 DTRTSAF-RDLQGQLAHAKKQQ--ELQQRYAELCAAAITCTAQCEKLEKIhlqESAQSLKEREQQLQTKEQIHLQETRKK 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 818 SEINLLTLEKVELERKLEsatKSKLHYKQQwgRALKELARLKQREQESQMARLKKQQEELEQMR-----LRYLAAEEKDT 892
Cdd:TIGR00618 490 AVVLARLLELQEEPCPLC---GSCIHPNPA--RQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYhqltsERKQRASLKEQ 564
|
250 260
....*....|....*....|....*
gi 1769843751 893 VKTERQELLDI---RNELNSDIKKT 914
Cdd:TIGR00618 565 MQEIQQSFSILtqcDNRSKEDIPNL 589
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
655-899 |
4.29e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.88 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 655 LELEMWKEMQEdiFENQLKQKELAhMQALAEEwKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQ 734
Cdd:pfam05557 105 VISCLKNELSE--LRRQIQRAELE-LQSTNSE-LEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQ 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 735 reKKELQSERQRNLQELQDSIRRAkedcihQVELERLK--IKQLEE---DKHRLQQQLNDAENKYKILEKEFQQFKDQQ- 808
Cdd:pfam05557 181 --SQEQDSEIVKNSKSELARIPEL------EKELERLRehNKHLNEnieNKLLLKEEVEDLKRKLEREEKYREEAATLEl 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 809 -NNKPEIRLQSEINLLTLEKVELeRKLEsATKSKLHYKQQWGRALKElarlKQREQESQMARLKKQQEELEQMRLRYLAA 887
Cdd:pfam05557 253 eKEKLEQELQSWVKLAQDTGLNL-RSPE-DLSRRIEQLQQREIVLKE----ENSSLTSSARQLEKARRELEQELAQYLKK 326
|
250
....*....|..
gi 1769843751 888 EEKDTVKTERQE 899
Cdd:pfam05557 327 IEDLNKKLKRHK 338
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
684-906 |
4.29e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 684 AEEWKKRDRERESLVKKKVAEYTILEgklQKTLIDLEKREQQLASVESELQREKKELQSERQRNLQElqdsIRRAKEDCI 763
Cdd:PTZ00121 1190 AEELRKAEDARKAEAARKAEEERKAE---EARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEE----IRKFEEARM 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 764 HQVELERLKIKQLEEDKhrlQQQLNDAENKYKilekefqqfKDQQNNKPEIRLQSEINlltlEKVELERKLESATKSKLH 843
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARK---ADELKKAEEKKK---------ADEAKKAEEKKKADEAK----KKAEEAKKADEAKKKAEE 1326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1769843751 844 YKQQwGRALKELARLKQREQESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNE 906
Cdd:PTZ00121 1327 AKKK-ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
653-882 |
4.56e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 653 AALELEMWKEMQEDIFENQLkqkELAHMQALAEEWKKRDRERESLVKKKVAEYTILEG-----KLQKTLIDLEKREQQLA 727
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVL---ELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAwqtarELLRRYRSQQALAQRLQ 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 728 SVESELQREKKELqsERQRNLQELQDSI-RRAKEDCIHQVELERLKiKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKD 806
Cdd:COG3096 516 QLRAQLAELEQRL--RQQQNAERLLEEFcQRIGQQLDAAEELEELL-AELEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1769843751 807 QQNnkpEIRLQSEINLLTLEKVElerKLESATKSKLHYKQQWGRALKELA-RLKQREQESQMARLKKQQEELEQMRL 882
Cdd:COG3096 593 RIK---ELAARAPAWLAAQDALE---RLREQSGEALADSQEVTAAMQQLLeREREATVERDELAARKQALESQIERL 663
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
718-914 |
4.81e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 718 DLEKREQQLASVESELQREKKELQSERQRNlQELQDSIRRAKEdcihqvELERL--KIKQLEEDKHRLQQQLNDAENKYK 795
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRT-ENIEELIKEKEK------ELEEVlrEINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 796 ILEKefqqfkdqqnnkpeirLQSEINlltlekvELERKLESATKSKlhykqqwgRALKElarlKQREQESQMARLKKQQE 875
Cdd:PRK03918 232 ELEE----------------LKEEIE-------ELEKELESLEGSK--------RKLEE----KIRELEERIEELKKEIE 276
|
170 180 190
....*....|....*....|....*....|....*....
gi 1769843751 876 ELEQMRLRYLAAEEKDTVKTERQELLDIRNELNSDIKKT 914
Cdd:PRK03918 277 ELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKR 315
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
646-911 |
4.93e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 646 RETLEyKAALELEMWKEMQEDIFEnqLKQkELAHMQALAEEwkkRDRERESLvKKKVAEytilegkLQKTLIDLEKREQQ 725
Cdd:PRK02224 233 RETRD-EADEVLEEHEERREELET--LEA-EIEDLRETIAE---TEREREEL-AEEVRD-------LRERLEELEEERDD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 726 LASvESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFqqfk 805
Cdd:PRK02224 298 LLA-EAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESEL---- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 806 dqQNNKPEIRLQSEinlltlEKVELERKLESATKSKLHYKQQWGRA-------LKELARLKQREQESQmARLKKQQEELE 878
Cdd:PRK02224 373 --EEAREAVEDRRE------EIEELEEEIEELRERFGDAPVDLGNAedfleelREERDELREREAELE-ATLRTARERVE 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1769843751 879 QMRlRYLAA-----------------------EEKDTVKTERQELLDIRNELNSDI 911
Cdd:PRK02224 444 EAE-ALLEAgkcpecgqpvegsphvetieedrERVEELEAELEDLEEEVEEVEERL 498
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
717-879 |
5.04e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 39.59 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 717 IDLEKREQQLASVESELQREKKELQSErQRNLQELQDSIRRAKEdcihqvelerlkikQLEEDKHRLQQ---QLNDAENK 793
Cdd:pfam12795 78 LSLEELEQRLLQTSAQLQELQNQLAQL-NSQLIELQTRPERAQQ--------------QLSEARQRLQQirnRLNGPAPP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 794 YKILEKEF-------QQFKDQQNNKPEIRLQSEINLLTLEKVELERklesaTKSKLHYKQQWGRALKE-LARLKQREQES 865
Cdd:pfam12795 143 GEPLSEAQrwalqaeLAALKAQIDMLEQELLSNNNRQDLLKARRDL-----LTLRIQRLEQQLQALQElLNEKRLQEAEQ 217
|
170
....*....|....
gi 1769843751 866 QMARLKKQQEELEQ 879
Cdd:pfam12795 218 AVAQTEQLAEEAAG 231
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
767-881 |
5.79e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 37.59 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 767 ELErLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQnnkpeIRLQSEINLLTLEKVELERKLESATKSKLHYKQ 846
Cdd:pfam20492 10 ELE-ERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEA-----ERLEQKRQEAEEEKERLEESAEMEAEEKEQLEA 83
|
90 100 110
....*....|....*....|....*....|....*
gi 1769843751 847 QWgRALKELARLKQREQESQMARLKKQQEELEQMR 881
Cdd:pfam20492 84 EL-AEAQEEIARLEEEVERKEEEARRLQEELEEAR 117
|
|
| Lipase_chap |
pfam03280 |
Proteobacterial lipase chaperone protein; |
716-892 |
5.84e-03 |
|
Proteobacterial lipase chaperone protein;
Pssm-ID: 427230 [Multi-domain] Cd Length: 185 Bit Score: 38.83 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 716 LIDLEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQleedkhrlQQQLNDAENKYK 795
Cdd:pfam03280 12 LAELDAPAPALGDSLAALRARLEQLQALRRRYFSPEEADALFGEEEAYDRYALERLAIAQ--------DSALSAEEKQQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 796 ILEKEFQQFKDQQNNKPEIRLQSEINLLTlekVELERKLESATKSKLHYKQQWGRALKE-LARLKQREQESQmARLKKQQ 874
Cdd:pfam03280 84 LAALRAQLPEDLRAAREAQQRLQELAART---AQLQKAGASPQQLRQARAQLVGPEAAQrLAALDQQRAAWQ-QRLDDYL 159
|
170
....*....|....*...
gi 1769843751 875 EELEQMRLRYLAAEEKDT 892
Cdd:pfam03280 160 AERQQINAAGLSEQERQA 177
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
680-758 |
6.48e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 37.94 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 680 MQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREK----KELQSERQRNLQELQDSI 755
Cdd:pfam03938 21 QAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQqkaqQELQKKQQELLQPIQDKI 100
|
...
gi 1769843751 756 RRA 758
Cdd:pfam03938 101 NKA 103
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
647-915 |
6.52e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.11 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 647 ETLEYKAALELEmwKEMQEDIFENQLkqkELAHMQALAEEWKKRDRERESLVKKKVAeytilegkLQKTLIDLEKREQQL 726
Cdd:pfam05557 229 EVEDLKRKLERE--EKYREEAATLEL---EKEKLEQELQSWVKLAQDTGLNLRSPED--------LSRRIEQLQQREIVL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 727 ASVESELQREKKELQSERQrnlqELQDSIRRAKEdcihQVELERLKIKQLEEDKHRLQQQ---LNDAENKYKILEKEFQq 803
Cdd:pfam05557 296 KEENSSLTSSARQLEKARR----ELEQELAQYLK----KIEDLNKKLKRHKALVRRLQRRvllLTKERDGYRAILESYD- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 804 fKDQQNNKPEIRLQSEINLLT--LEKV-----ELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEE 876
Cdd:pfam05557 367 -KELTMSNYSPQLLERIEEAEdmTQKMqahneEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDS 445
|
250 260 270
....*....|....*....|....*....|....*....
gi 1769843751 877 LEQmrlrylaaeEKDTVKTERQELLDIRNELNSDIKKTN 915
Cdd:pfam05557 446 LRR---------KLETLELERQRLREQKNELEMELERRC 475
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
711-912 |
6.60e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 711 KLQKTLIDLEKREQQLASVESELQREKKELQsERQRNLQELQDSIRRaKEDCIHQV--ELERLK--------------IK 774
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLS-EKQKELEQNNKKIKE-LEKQLNQLksEISDLNnqkeqdwnkelkseLK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 775 QLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKpeirlQSEINLLTLEKVELERKLESATKSKLHYKQQwgraLKE 854
Cdd:TIGR04523 318 NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNS-----ESENSEKQRELEEKQNEIEKLKKENQSYKQE----IKN 388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1769843751 855 LaRLKQREQESQMARLKKQQEELEQmRLRYLaAEEKDTVKTERQELLDIRNELNSDIK 912
Cdd:TIGR04523 389 L-ESQINDLESKIQNQEKLNQQKDE-QIKKL-QQEKELLEKEIERLKETIIKNNSEIK 443
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
642-888 |
6.82e-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: 40.34 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 642 QTEPRETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEK 721
Cdd:TIGR00618 657 QERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 722 REQQLASVESELQREKKELQSER-----QRNLQELQDSIRRAKEDciHQVELERLKIKQLEEDKHRLQQQLNDAENKYK- 795
Cdd:TIGR00618 737 REDALNQSLKELMHQARTVLKARteahfNNNEEVTAALQTGAELS--HLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPs 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 796 -ILEKEFQQFKDQQnnkpeiRLQSEINLLTlekvELERKLESATKSKLHY---KQQWGRALKELARLKQREQESQMARLK 871
Cdd:TIGR00618 815 dEDILNLQCETLVQ------EEEQFLSRLE----EKSATLGEITHQLLKYeecSKQLAQLTQEQAKIIQLSDKLNGINQI 884
|
250
....*....|....*..
gi 1769843751 872 KQQeeLEQMRLRYLAAE 888
Cdd:TIGR00618 885 KIQ--FDGDALIKFLHE 899
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
700-893 |
8.39e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 39.85 E-value: 8.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 700 KKVAEYTILEGKLQKTLIdlekREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLE-- 777
Cdd:PRK00106 30 KEAAELTLLNAEQEAVNL----RGKAERDAEHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSERQELKQIEsr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 778 --EDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIRLQSEiNLLTLEKVELER--KLESATKSKLHYKQQWGRALK 853
Cdd:PRK00106 106 ltERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDEREEQVE-KLEEQKKAELERvaALSQAEAREIILAETENKLTH 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1769843751 854 ELA-RLKQREQESQMARLKKQQEELEQMRLR----YLAAEEKDTV 893
Cdd:PRK00106 185 EIAtRIREAEREVKDRSDKMAKDLLAQAMQRlageYVTEQTITTV 229
|
|
| DUF4472 |
pfam14739 |
Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members ... |
709-810 |
8.51e-03 |
|
Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members also carry Kinesin-motor domains at their N-terminus, Kinesin, pfam00225.
Pssm-ID: 464291 [Multi-domain] Cd Length: 107 Bit Score: 36.90 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 709 EGKLQ--KTLIDLEKREQQLasvESELQREKKELQSERQR---NLQELQdsIRRAKEDCIHQVELERLKIkqLEEDKHRL 783
Cdd:pfam14739 3 EEKLQisKALVDLQIENNKL---REQYEAEKFELKNKLLNlenRVLELE--LRLEKAAEEIQDLRERLRE--LEDDRREL 75
|
90 100
....*....|....*....|....*..
gi 1769843751 784 QQQLNDAENKYKILEKEFQQFKDQQNN 810
Cdd:pfam14739 76 AEEFVALKKNYQALSKELEAEVAKNQE 102
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
668-913 |
9.44e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 39.70 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 668 FENQLKQKE-LAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVEselqrEKKELQSERQR 746
Cdd:pfam05483 211 LEMHFKLKEdHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLE-----EKTKLQDENLK 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 747 NLQELQDSIRRAKEDCIHQVELERLKIKQLEED---------------------------KHRL---------------- 783
Cdd:pfam05483 286 ELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDlqiatkticqlteekeaqmeelnkakaAHSFvvtefeattcsleell 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843751 784 ---QQQLNDAENKYKILEKEFQQFKDQQNNKPEIRLQSEINLLTLEKVELErklesatKSKLHYKQQWGRALKElaRLKQ 860
Cdd:pfam05483 366 rteQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE-------DEKLLDEKKQFEKIAE--ELKG 436
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1769843751 861 REQEsQMARLKKQQEELEQMRLRYLAaeekdtVKTERQELLDIRNELNSDIKK 913
Cdd:pfam05483 437 KEQE-LIFLLQAREKEIHDLEIQLTA------IKTSEEHYLKEVEDLKTELEK 482
|
|
| |
