|
Name |
Accession |
Description |
Interval |
E-value |
| RBD-FIP |
pfam09457 |
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ... |
761-801 |
7.47e-16 |
|
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.
Pssm-ID: 462805 [Multi-domain] Cd Length: 41 Bit Score: 71.60 E-value: 7.47e-16
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1634229844 761 SRDELMEAIQKQEEINFRLQDYIDRIIVAIMETNPSILEVK 801
Cdd:pfam09457 1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
515-787 |
8.42e-15 |
|
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: 78.95 E-value: 8.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 515 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQL---------KEQELRACEMVLEETRRQKELLCKMEREKSIE 585
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELeqlrkeleeLSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 586 IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDR---LSHERHQFQRDKEA 662
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 663 TQELIEDLRKQLEHL--QLLKLEAEQRRGRSS--------------SMGLQEYHSRARE--SELEQEVRRLKQDNRNLKE 724
Cdd:TIGR02168 836 TERRLEDLEEQIEELseDIESLAAEIEELEELieeleseleallneRASLEEALALLRSelEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1634229844 725 QNEELNGQI--ITLSIQGAKSLFstafsESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRII 787
Cdd:TIGR02168 916 ELEELREKLaqLELRLEGLEVRI-----DNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
504-781 |
2.33e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 504 EEDIADKVVFLeRRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKEllckmEREKS 583
Cdd:COG1196 221 ELKELEAELLL-LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-----EYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 584 IEIENLQTRLQQLDEENSELRsctpclkANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEAT 663
Cdd:COG1196 295 AELARLEQDIARLEERRRELE-------ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 664 QELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKS 743
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270
....*....|....*....|....*....|....*...
gi 1634229844 744 LFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQD 781
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
509-782 |
5.83e-13 |
|
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: 72.79 E-value: 5.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 509 DKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRAcEMVLEETRRQKEllckmereksiEIEN 588
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI-EQLEQEEEKLKE-----------RLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 589 LQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQ------------ENKRRMGDRLSH----- 651
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelskleEEVSRIEARLREieqkl 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 652 ------------ERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSsmgLQEYHSRARESELEQEVRRLKQDN 719
Cdd:TIGR02169 822 nrltlekeylekEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE---AALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 720 RNLKEQNEELNGQIITLSIQGA--KSLFSTAFS-----ESLAAEISSVS------------RDELMEAIQKQEEINFR-L 779
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSelKAKLEALEEelseiEDPKGEDEEIPeeelsledvqaeLQRVEEEIRALEPVNMLaI 978
|
...
gi 1634229844 780 QDY 782
Cdd:TIGR02169 979 QEY 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
536-785 |
2.98e-12 |
|
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: 70.47 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 536 RQENLQLVHRANA---LEEQLKEQE--LRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCL 610
Cdd:TIGR02168 666 AKTNSSILERRREieeLEEKIEELEekIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 611 KANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGR 690
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 691 SSSMglqeyhsRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKS-------LFSTAFSESLAAEISSvSRD 763
Cdd:TIGR02168 826 LESL-------ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELeselealLNERASLEEALALLRS-ELE 897
|
250 260
....*....|....*....|..
gi 1634229844 764 ELMEAIQKQEEINFRLQDYIDR 785
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEE 919
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
545-739 |
3.08e-12 |
|
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: 70.47 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 545 RANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKL 624
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 625 LDEIESLTLR---LSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQlLKLEAEQRRGRSSSMGLQEYHS 701
Cdd:TIGR02168 294 ANEISRLEQQkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK-EELESLEAELEELEAELEELES 372
|
170 180 190
....*....|....*....|....*....|....*...
gi 1634229844 702 RAResELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQ 739
Cdd:TIGR02168 373 RLE--ELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
450-774 |
4.57e-12 |
|
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: 70.09 E-value: 4.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 450 INRLEDLsarLSDLEMNSPTKRLSSKKVARYLHQSgaltmEALEDPSPELmegpeedIADKVVFLERRVLELEKDTAATG 529
Cdd:TIGR02168 188 LDRLEDI---LNELERQLKSLERQAEKAERYKELK-----AELRELELAL-------LVLRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 530 EQHSRLRQEnlqlvhrANALEEQLKEQELRACEMVLEETRRQKELL------CKMEREKSI---EIENLQTRLQQLDEEN 600
Cdd:TIGR02168 253 EELEELTAE-------LQELEEKLEELRLEVSELEEEIEELQKELYalaneiSRLEQQKQIlreRLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 601 SELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEE----QENKRRMGD------RLSHERHQFQRDKEATQELIEDL 670
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELeaelEELESRLEEleeqleTLRSKVAQLELQIASLNNEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 671 RKQLEHlqllkLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKSlfSTAFS 750
Cdd:TIGR02168 406 EARLER-----LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA--EQALD 478
|
330 340
....*....|....*....|....
gi 1634229844 751 ESLAAEISSVSRDELMEAIQKQEE 774
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
505-785 |
8.88e-12 |
|
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: 68.93 E-value: 8.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 505 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELracEMVLEETRRQKELLCKMEREKSI 584
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA---EIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 585 E-----IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFqrd 659
Cdd:TIGR02168 785 EeleaqIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI--- 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 660 kEATQELIEDLRKQLEHL----------------QLLKLEAEQRRGRSSSMGLQEYHSRARES---------ELEQEVRR 714
Cdd:TIGR02168 862 -EELEELIEELESELEALlnerasleealallrsELEELSEELRELESKRSELRRELEELREKlaqlelrleGLEVRIDN 940
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1634229844 715 LKQdnrNLKEQneelngQIITLSIQGAKSLFSTAFSESLAAEISSVSR--DEL----MEAIQKQEEINFRLqDYIDR 785
Cdd:TIGR02168 941 LQE---RLSEE------YSLTLEEAEALENKIEDDEEEARRRLKRLENkiKELgpvnLAAIEEYEELKERY-DFLTA 1007
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
505-774 |
8.11e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 8.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 505 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANAL--EEQLKEQELRACEMVLEETRRQKELLCKMEREK 582
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 583 SIEIENLQTRL----QQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRrmgdrlshERHQFQR 658
Cdd:COG1196 322 EEELAELEEELeeleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE--------ELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 659 DKEATQELIEDLRKQLEHLQLLKLEAEQRRGRsssmgLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSI 738
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEE-----LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260 270
....*....|....*....|....*....|....*.
gi 1634229844 739 QGAKSLFSTAFSESLAAEISSVSRDELMEAIQKQEE 774
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
504-742 |
1.21e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 504 EEDIADKVVFLERRVLELEKdtaaTGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEEtrrqKELLCKMEREKs 583
Cdd:PRK03918 216 LPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI----EELEEKVKELK- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 584 iEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEK---QKLLDEIESLTLRLSEEQENKRRMGDRLS--HERHQFQR 658
Cdd:PRK03918 287 -ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngiEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 659 DKEATQELIEDLRKQLEHLQLLKLEAEQrrgrsssmglqEYHSRAREsELEQEVRRLKQDNRNLKEQNEELNGQIITLsi 738
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKEL-----------EELEKAKE-EIEEEISKITARIGELKKEIKELKKAIEEL-- 431
|
....
gi 1634229844 739 QGAK 742
Cdd:PRK03918 432 KKAK 435
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
517-793 |
2.48e-09 |
|
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: 60.80 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 517 RVLELEKDTAAtgEQHSRLRQENLQ-------LVHRANALEEQLK---------EQELRACEMVLEETRRQKELLCKMER 580
Cdd:TIGR04523 415 KKLQQEKELLE--KEIERLKETIIKnnseikdLTNQDSVKELIIKnldntreslETQLKVLSRSINKIKQNLEQKQKELK 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 581 EKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRmgDRLSHERHQFQRDK 660
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK--ENLEKEIDEKNKEI 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 661 EATQELIEDLRKQLEHLQLL--KLEAEQRRGRSssmGLQEYHSRAreSELEQEVrrlkqdnRNLKEQNEELNGQIITlsI 738
Cdd:TIGR04523 571 EELKQTQKSLKKKQEEKQELidQKEKEKKDLIK---EIEEKEKKI--SSLEKEL-------EKAKKENEKLSSIIKN--I 636
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1634229844 739 QGAKslfstafsESLAAEISSVsRDELMEAIQKQEEINFRLQDYIDRI--IVAIMET 793
Cdd:TIGR04523 637 KSKK--------NKLKQEVKQI-KETIKEIRNKWPEIIKKIKESKTKIddIIELMKD 684
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
505-729 |
3.02e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 505 EDIADKVVFLERRVLELEKdtaaTGEQHSRLRQeNLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREksi 584
Cdd:PRK03918 469 KEIEEKERKLRKELRELEK----VLKKESELIK-LKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE--- 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 585 eIENLQTRLQQLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENK---------------------R 643
Cdd:PRK03918 541 -IKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELEELGFESVEELEERlkelepfyneylelkdaekelE 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 644 RMGDRLSHERHQFQRDKEATQEL---IEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARE--SELEQEVRRLKQD 718
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETekrLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAelEELEKRREEIKKT 695
|
250
....*....|.
gi 1634229844 719 NRNLKEQNEEL 729
Cdd:PRK03918 696 LEKLKEELEER 706
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
514-801 |
3.12e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.53 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 514 LERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLkeQELRAcemVLEETRRQKELLCKMEREKSIEIENLQTRL 593
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEEL--EQLRE---ELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 594 QQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIEsltlRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQ 673
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELE----ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 674 LEHLQllkleAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKSLFSTAFSESL 753
Cdd:COG4372 159 LESLQ-----EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1634229844 754 AAEISSVSRDELMEAIQKQEEINFRLQDYIDRIIVAIMETNPSILEVK 801
Cdd:COG4372 234 ALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIA 281
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
508-718 |
3.14e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 508 ADKVVFLERRVLELEKDTAATGEQHSRLRQEnlqlvhrANALEEQlkeqeLRACEMVLEETRRQKELlckmeREKSIEIE 587
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAE-------LDALQER-----REALQRLAEYSWDEIDV-----ASAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 588 NLQTRLQQLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQR-DKEATQEL 666
Cdd:COG4913 672 ELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLEL 747
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1634229844 667 IEDLRKQLEHLQLLKLEAEQRRG-RSSSMGLQEYHSRAREsELEQEVRRLKQD 718
Cdd:COG4913 748 RALLEERFAAALGDAVERELRENlEERIDALRARLNRAEE-ELERAMRAFNRE 799
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
452-733 |
9.09e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 9.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 452 RLEDLSARLSDLEMNspTKRLSS--KKVARYLHQSGALT--------MEALEDPSPELMEGPEEDIAD------KVVFLE 515
Cdd:PRK03918 267 RIEELKKEIEELEEK--VKELKElkEKAEEYIKLSEFYEeyldelreIEKRLSRLEEEINGIEERIKEleekeeRLEELK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 516 RRVLELEKDTAATGEQHsRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQ 595
Cdd:PRK03918 345 KKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 596 LDEENSELRS----CTPC---------------LKANIERLEEEKQKLLDEIESLTLRLsEEQENKRRMGDRLSHERHQF 656
Cdd:PRK03918 424 LKKAIEELKKakgkCPVCgrelteehrkelleeYTAELKRIEKELKEIEEKERKLRKEL-RELEKVLKKESELIKLKELA 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 657 QRDKEATQEL----IEDLRKQLEHLQLLKLEAEQRRGRSSSMGlqeyHSRARESELEQEVRRLKQDNRNLKEQNEELNGQ 732
Cdd:PRK03918 503 EQLKELEEKLkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLK----KELEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
.
gi 1634229844 733 I 733
Cdd:PRK03918 579 L 579
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
451-729 |
1.39e-08 |
|
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: 58.81 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 451 NRLEDLSARLSDLEMNSPTKRLSSKKVARyLHQSGA------LTMEALEDPSPELMEgpeedIADKVVFLERrvlELEKD 524
Cdd:COG3096 785 KRLEELRAERDELAEQYAKASFDVQKLQR-LHQAFSqfvgghLAVAFAPDPEAELAA-----LRQRRSELER---ELAQH 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 525 TAATGEQHSRLRQ--ENLQLVHR----ANALEEQLKEQELRACEMVLEE-------TRRQKELLCKMEREKSI------E 585
Cdd:COG3096 856 RAQEQQLRQQLDQlkEQLQLLNKllpqANLLADETLADRLEELREELDAaqeaqafIQQHGKALAQLEPLVAVlqsdpeQ 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 586 IENLQTRLQQLDEENSELRSCTPCLKANIERLE----EEKQKLLDE----IESLTLRLSEEQENKRRMGDRLSHERHQFQ 657
Cdd:COG3096 936 FEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGEnsdlNEKLRARLEQAEEARREAREQLRQAQAQYS 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 658 rdkEATQELI----------EDLRKQLEHLQLLKL----EAEQR-RGRSSSMGLQEYHSRAR-----------ESELEQE 711
Cdd:COG3096 1016 ---QYNQVLAslkssrdakqQTLQELEQELEELGVqadaEAEERaRIRRDELHEELSQNRSRrsqlekqltrcEAEMDSL 1092
|
330
....*....|....*...
gi 1634229844 712 VRRLKQDNRNLKEQNEEL 729
Cdd:COG3096 1093 QKRLRKAERDYKQEREQV 1110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
534-786 |
1.54e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 534 RLR--QENLQlvhRANALEEQLKEQelracemvLEETRRQKEllcKMER--EKSIEIENLQTRLQQLDEENselrsctpc 609
Cdd:COG1196 180 KLEatEENLE---RLEDILGELERQ--------LEPLERQAE---KAERyrELKEELKELEAELLLLKLRE--------- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 610 LKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQEL---IEDLRKQLEHLQLLKLEAEQ 686
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELlaeLARLEQDIARLEERRRELEE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 687 RRGRsssMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLsiQGAKSLFSTAFSESLAAEISsvSRDELM 766
Cdd:COG1196 317 RLEE---LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA--EEALLEAEAELAEAEEELEE--LAEELL 389
|
250 260
....*....|....*....|
gi 1634229844 767 EAIQKQEEINFRLQDYIDRI 786
Cdd:COG1196 390 EALRAAAELAAQLEELEEAE 409
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
516-736 |
2.68e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.44 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 516 RRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEmvlEETRRQKELLCKMEREKSIEIEnlqtRLQQ 595
Cdd:pfam17380 395 RQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLE---EERAREMERVRLEEQERQQQVE----RLRQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 596 LDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLE 675
Cdd:pfam17380 468 QEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQE 547
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1634229844 676 HlqllkleAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNlKEQNEELNGQIITL 736
Cdd:pfam17380 548 M-------EERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK-ARAEYEATTPITTI 600
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
515-786 |
3.79e-08 |
|
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: 57.39 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 515 ERRVLELEKDTAATGEQHSRLRQENLQLVhRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQ 594
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 595 QLDEENSELRSCTPCLKANIERL-EEEKQKLLDEIESLTLRLSE----EQENKRRMGDrLSHERHQFQRDKEATQELIED 669
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASlersIAEKERELED-AEERLAKLEAEIDKLLAEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 670 LRKQLEHLQLLK-----------------------LEAEQRRGRSSSMGLQEYHSRARE--SELEQEVRRLKQDNRNLKE 724
Cdd:TIGR02169 341 LEREIEEERKRRdklteeyaelkeeledlraeleeVDKEFAETRDELKDYREKLEKLKReiNELKRELDRLQEELQRLSE 420
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1634229844 725 QNEELNGQIItlSIQGAKSLFSTAfSESLAAEISSvSRDELMEAIQKQEEIN---FRLQDYIDRI 786
Cdd:TIGR02169 421 ELADLNAAIA--GIEAKINELEEE-KEDKALEIKK-QEWKLEQLAADLSKYEqelYDLKEEYDRV 481
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
530-733 |
4.45e-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: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 530 EQHSRLrQENLQLVHRANALEEQLKEQElracemvleetrrqkellcKMEREKSIEIENLQTRLQQLDEENSELRSCTPC 609
Cdd:TIGR04523 378 ENQSYK-QEIKNLESQINDLESKIQNQE-------------------KLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 610 LKANIERLEEEKQKLLDEIESLTlRLSEEQENKRrmgDRLSHERHQFQRDKEATQELIEDLRKqlehlQLLKLEAEQrrg 689
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLD-NTRESLETQL---KVLSRSINKIKQNLEQKQKELKSKEK-----ELKKLNEEK--- 505
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1634229844 690 rsssmglqeyhsrareSELEQEVRRLKQDNRNLKEQNEELNGQI 733
Cdd:TIGR04523 506 ----------------KELEEKVKDLTKKISSLKEKIEKLESEK 533
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
486-733 |
4.98e-08 |
|
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: 57.00 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 486 ALTMEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQ--ELRACEM 563
Cdd:TIGR02169 264 EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLlaEIEELER 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 564 VLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESL---TLRLSEEQE 640
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeeLQRLSEELA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 641 NKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQ--LLKLEAEQRRGRSSSMGLQ-EYHSRARE-SELEQEVRRLK 716
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAadLSKYEQELYDLKEEYDRVEkELSKLQRElAEAEAQARASE 503
|
250
....*....|....*..
gi 1634229844 717 QDNRNLKEQNEELNGQI 733
Cdd:TIGR02169 504 ERVRGGRAVEEVLKASI 520
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
505-776 |
7.82e-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: 56.18 E-value: 7.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 505 EDIADKvvflERRVLELEKDTAATGEQHSRLRQEnlqlvhrANALEEQLKEQELracemvlEETRRQKELlckmeREKSI 584
Cdd:TIGR04523 314 SELKNQ----EKKLEEIQNQISQNNKIISQLNEQ-------ISQLKKELTNSES-------ENSEKQREL-----EEKQN 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 585 EIE---------------------NLQTRLQQLDEENSELRSctpclkaNIERLEEEKQKLLDEIEsltlRLSEEQENKR 643
Cdd:TIGR04523 371 EIEklkkenqsykqeiknlesqinDLESKIQNQEKLNQQKDE-------QIKKLQQEKELLEKEIE----RLKETIIKNN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 644 RMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQL----LKLEAEQRRgrsssmglQEYHSRARE-SELEQEVRRLKQD 718
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRsinkIKQNLEQKQ--------KELKSKEKElKKLNEEKKELEEK 511
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1634229844 719 NRNLKEQNEELNGQIITLSIQgaKSLFSTAFSeSLAAEISS----VSRDELMEAIQ-KQEEIN 776
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESE--KKEKESKIS-DLEDELNKddfeLKKENLEKEIDeKNKEIE 571
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
525-743 |
8.12e-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: 55.16 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 525 TAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMV--LEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSE 602
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLkqLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 603 LRsctpclkANIERLEEEKQKLLDEI------ESLTLRLSEEQENK--------RRMGDRLSHERHQFQRDKEATQELIE 668
Cdd:COG4942 95 LR-------AELEAQKEELAELLRALyrlgrqPPLALLLSPEDFLDavrrlqylKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1634229844 669 DLRKQLEHLQLLKLEAEQRRGRsssmgLQEYHSRARE--SELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKS 743
Cdd:COG4942 168 ELEAERAELEALLAELEEERAA-----LEALKAERQKllARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
206-264 |
8.54e-08 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 49.56 E-value: 8.54e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1634229844 206 RLRAVFDALDGDGDGFVRIEDFIQFATVYGA------EQVKDLTKYLDPSGLGVISFEDFYQGIT 264
Cdd:pfam13499 3 KLKEAFKLLDSDGDGYLDVEELKKLLRKLEEgeplsdEEVEELFKEFDLDKDGRISFEEFLELYS 67
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
201-264 |
1.09e-07 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 51.72 E-value: 1.09e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1634229844 201 QEDGPRLRAVFDALDGDGDGFVRIEDFIQFATVYG--AEQVKDLTKYLDPSGLGVISFEDFYQGIT 264
Cdd:COG5126 65 ATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGvsEEEADELFARLDTDGDGKISFEEFVAAVR 130
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
545-733 |
1.26e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 545 RANALEEQLkeQELRACEMVLEETRRQKELLCKMeREKSIEIENLQTRLQQLDEENSELRS-----CTPCLKANIERLEE 619
Cdd:COG4913 226 AADALVEHF--DDLERAHEALEDAREQIELLEPI-RELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 620 EKQKLLDEIESLTLRLSEEQENKRRMgdRLSHERHQFQRdkeatqelIEDLRKQLEHLQLLKLEAEQRRGR--------- 690
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDEL--EAQIRGNGGDR--------LEQLEREIERLERELEERERRRARleallaalg 372
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1634229844 691 ----SSSMGLQEYHSRARE---------SELEQEVRRLKQDNRNLKEQNEELNGQI 733
Cdd:COG4913 373 lplpASAEEFAALRAEAAAllealeeelEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
499-731 |
1.31e-07 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 54.69 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 499 LMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKE--QELRACEMVLEETRRQKELLC 576
Cdd:pfam19220 31 QLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEElvARLAKLEAALREAEAAKEELR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 577 KMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLseeqenkrrmgDRLSHERHQF 656
Cdd:pfam19220 111 IELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERL-----------ALLEQENRRL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1634229844 657 Q-RDKEATQELIEDLRKQLEHLQLlkLEAEQRRGR---SSSMGLQEYHSRArESELEQEVRRLKQDNRNLKEQNEELNG 731
Cdd:pfam19220 180 QaLSEEQAAELAELTRRLAELETQ--LDATRARLRaleGQLAAEQAERERA-EAQLEEAVEAHRAERASLRMKLEALTA 255
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
451-731 |
1.52e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 451 NRLEDLSARLSDLEmnsptKRLSSKKVARYLHQSGALTMEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTAATGE 530
Cdd:PRK03918 338 ERLEELKKKLKELE-----KRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 531 QHSRLRQENLQLVHRANALEEqlKEQELRACEMVLEETRRqKELLckmeREKSIEIENLQTRLQQLDEENSELRSctPCL 610
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKK--AKGKCPVCGRELTEEHR-KELL----EEYTAELKRIEKELKEIEEKERKLRK--ELR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 611 KANIERLEEEK----QKLLDEIESLTLRLS-----------EEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLE 675
Cdd:PRK03918 484 ELEKVLKKESEliklKELAEQLKELEEKLKkynleelekkaEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK 563
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1634229844 676 HLQLLKLEAEQRRGRSSSMG-------------LQEYHSR-----ARESELEQEVRRLKQDNRNLKEQNEELNG 731
Cdd:PRK03918 564 KLDELEEELAELLKELEELGfesveeleerlkeLEPFYNEylelkDAEKELEREEKELKKLEEELDKAFEELAE 637
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
520-784 |
1.57e-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: 55.36 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 520 ELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEE 599
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 600 NSELRSCTpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRmgdrlsHERHQFQRDKEATQELIEDLRKQLEHLQL 679
Cdd:pfam02463 261 EKEEEKLA--QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL------KLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 680 LKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQ-DNRNLKEQNEELNGQIITLSIQG-AKSLFSTAFSE-SLAAE 756
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQlEEELLAKKKLESERLSSAAKLKEeELELKSEEEKEaQLLLE 412
|
250 260
....*....|....*....|....*...
gi 1634229844 757 ISSVSRDELMEAIQKQEEINFRLQDYID 784
Cdd:pfam02463 413 LARQLEDLLKEEKKEELEILEEEEESIE 440
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
504-716 |
2.66e-07 |
|
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: 53.61 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 504 EEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQElracemvlEETRRQKELLCKMEREKS 583
Cdd:COG4942 50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK--------EELAELLRALYRLGRQPP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 584 IEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEkqklLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEAT 663
Cdd:COG4942 122 LALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAELEALLAELEEERAALEALKAER 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1634229844 664 QELIEDLRKQLEHL--QLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLK 716
Cdd:COG4942 198 QKLLARLEKELAELaaELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
533-739 |
3.06e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 533 SRLRQENLQLvHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSI---EIENLQTRLQQLDEENSELRsctpc 609
Cdd:COG4717 49 ERLEKEADEL-FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEEleeELEELEAELEELREELEKLE----- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 610 LKANIERLEEEKQKLLDEIESLTLRLsEEQENKRRmgdrlshERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRG 689
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERL-EELEERLE-------ELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1634229844 690 RSSSMGLQEyhSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQ 739
Cdd:COG4717 195 QDLAEELEE--LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
509-786 |
3.28e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 509 DKVVFLERRVLELEKDTAATGEQHSRLRQENLQLvhraNALEEQLKEQELRacemvLEETRRQKELLCKMEREKSIEIEN 588
Cdd:COG4913 654 AEYSWDEIDVASAEREIAELEAELERLDASSDDL----AALEEQLEELEAE-----LEELEEELDELKGEIGRLEKELEQ 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 589 LQTRLQQLDEENSELRSctPCLKANIERLEEEKQKLLDE------IESLTLRLSEEQENKRRMGDRLSHERHQFQRD-KE 661
Cdd:COG4913 725 AEEELDELQDRLEAAED--LARLELRALLEERFAAALGDaverelRENLEERIDALRARLNRAEEELERAMRAFNREwPA 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 662 ATQELIEDLRKQLEHLQLL-KLEAEqrrgrsssmGLQEYHSRARESELEQE-------VRRLKQDNRNLKEQNEELN--- 730
Cdd:COG4913 803 ETADLDADLESLPEYLALLdRLEED---------GLPEYEERFKELLNENSiefvadlLSKLRRAIREIKERIDPLNdsl 873
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1634229844 731 -------GQIITLSIQGAKSLFSTAFSESLAAEISSVSRDElMEAIQKQEEinfRLQDYIDRI 786
Cdd:COG4913 874 kripfgpGRYLRLEARPRPDPEVREFRQELRAVTSGASLFD-EELSEARFA---ALKRLIERL 932
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
450-741 |
3.53e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 450 INRLE-DLSARLSDLEMNSPTKRLSSKKVARYLHQSGALTMeALEDPSPELMEgpeeDIADKVV--FLERRvLELEKDTA 526
Cdd:COG3206 100 VDKLNlDEDPLGEEASREAAIERLRKNLTVEPVKGSNVIEI-SYTSPDPELAA----AVANALAeaYLEQN-LELRREEA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 527 ATgeqhsrlrqenlqlvhRANALEEQLKE--QELRACEMVLEETRRQKELLCKMEREKSI--EIENLQTRLQQLDEENSE 602
Cdd:COG3206 174 RK----------------ALEFLEEQLPElrKELEEAEAALEEFRQKNGLVDLSEEAKLLlqQLSELESQLAEARAELAE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 603 LRSCTPCLKANIERLEEEKQKLLD--EIESLTLRLSEEQENKRRMGDRLShERHQfqrDKEATQELIEDLRKQLEH---- 676
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYT-PNHP---DVIALRAQIAALRAQLQQeaqr 313
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1634229844 677 -LQLLKLEAEQRRGRSSSMG--LQEYHSRARE-SELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGA 741
Cdd:COG3206 314 iLASLEAELEALQAREASLQaqLAQLEARLAElPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
514-774 |
7.42e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.05 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 514 LERRVLELEKdTAATGEQHSRLRQENLQLVHRANALEEQLKE----QELRACEMVLEETRRQKELLCKMEREKSIEIENl 589
Cdd:TIGR00618 417 SAFRDLQGQL-AHAKKQQELQQRYAELCAAAITCTAQCEKLEkihlQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA- 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 590 qtRLQQLDEENSELrsCTPCLKANIER----LEEEKQKLLDEIESLTLRLSEEQENKRRMGDRlshERHQFQRDKEATQE 665
Cdd:TIGR00618 495 --RLLELQEEPCPL--CGSCIHPNPARqdidNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTS---ERKQRASLKEQMQE 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 666 LIEDLRKQLEHLQLLKLEAEqrrgrsssmGLQEYHSRAR---ESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQgak 742
Cdd:TIGR00618 568 IQQSFSILTQCDNRSKEDIP---------NLQNITVRLQdltEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQ--- 635
|
250 260 270
....*....|....*....|....*....|..
gi 1634229844 743 slfstAFSESLAAEISSVSRDELMEAIQKQEE 774
Cdd:TIGR00618 636 -----QCSQELALKLTALHALQLTLTQERVRE 662
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
451-732 |
7.53e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.04 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 451 NRLEDLSARLSDLEMNSPTKRLSSKKVARyLHQSG--------ALTMEAleDPSPELmegpeEDIADKVVFLERRVLELE 522
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLSFDVQKLQR-LHQAFsrfigshlAVAFEA--DPEAEL-----RQLNRRRVELERALADHE 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 523 kdtAATGEQHSRLRQ--ENLQLVHR----ANALEEQLKEQELRACEMVLEET-------RRQKELLCKMEREKSI----- 584
Cdd:PRK04863 858 ---SQEQQQRSQLEQakEGLSALNRllprLNLLADETLADRVEEIREQLDEAeeakrfvQQHGNALAQLEPIVSVlqsdp 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 585 -EIENLQTRLQQLDEENSELRSCTPCLKANIERLE----EEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQ-R 658
Cdd:PRK04863 935 eQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQaQ 1014
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 659 DKEATQELI---------EDLRKQLEH-LQLLKL----EAEQR-RGRSSSMGLQEYHSRAR-----------ESELEQEV 712
Cdd:PRK04863 1015 LAQYNQVLAslkssydakRQMLQELKQeLQDLGVpadsGAEERaRARRDELHARLSANRSRrnqlekqltfcEAEMDNLT 1094
|
330 340
....*....|....*....|
gi 1634229844 713 RRLKQDNRNLKEQNEELNGQ 732
Cdd:PRK04863 1095 KKLRKLERDYHEMREQVVNA 1114
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
564-730 |
7.69e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 564 VLEETRRQKELLCK-MEREKSIE--IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKL---LDEIESLTLRLSE 637
Cdd:PRK03918 170 VIKEIKRRIERLEKfIKRTENIEelIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 638 EQENKRRMGDRLSherhQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMglQEYhsRARESELEQEVRRLKQ 717
Cdd:PRK03918 250 LEGSKRKLEEKIR----ELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFY--EEY--LDELREIEKRLSRLEE 321
|
170
....*....|...
gi 1634229844 718 DNRNLKEQNEELN 730
Cdd:PRK03918 322 EINGIEERIKELE 334
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
515-688 |
8.63e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 8.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 515 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEEtrrqkellckmereksiEIENLQTRLQ 594
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA-----------------ELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 595 QLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENK-RRMGDRLSH---ERHQFQRDKEATQELIEDL 670
Cdd:COG4717 150 ELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEElqqRLAELEEELEEAQEELEEL 225
|
170
....*....|....*...
gi 1634229844 671 RKQLEHLQLLKLEAEQRR 688
Cdd:COG4717 226 EEELEQLENELEAAALEE 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
514-741 |
1.02e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 514 LERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKE--QELRACEMVLEETRRQKELLCKMEREKSIEIEnLQT 591
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAElqEELEELEEELEELEAELEELREELEKLEKLLQ-LLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 592 RLQQLDEENSELRSCTPCLKANIERLEEEKQkLLDEIESLTLRLSEEQEnkrrmgdrlsHERHQFQRDKEATQELIEDLR 671
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRE-LEEELEELEAELAELQE----------ELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 672 KQLEHLQLLKLEAEQRRGRsssmglqeyhSRARESELEQEVRRLKQDNRNLKEQnEELNGQIITLSIQGA 741
Cdd:COG4717 199 EELEELQQRLAELEEELEE----------AQEELEELEEELEQLENELEAAALE-ERLKEARLLLLIAAA 257
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
515-727 |
1.04e-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: 52.44 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 515 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQElRACEMVLEETRRQK---ELLCKMEREKSieienlqT 591
Cdd:pfam05557 26 KRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAE-EALREQAELNRLKKkylEALNKKLNEKE-------S 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 592 RLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEdlr 671
Cdd:pfam05557 98 QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKE--- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1634229844 672 kqlehlqllkLEAEQRRGRSSSMGLQEYHSR-ARESELEQEVRRLKQDNRNLKEQNE 727
Cdd:pfam05557 175 ----------LEFEIQSQEQDSEIVKNSKSElARIPELEKELERLREHNKHLNENIE 221
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
504-728 |
1.32e-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: 51.07 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 504 EEDIADKVVFLERRvlelekdtAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMvLEETRRQKELLCKMEREks 583
Cdd:pfam13868 41 EERRLDEMMEEERE--------RALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEE-YEEKLQEREQMDEIVER-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 584 IEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESL--TLRLSEEQENKRRmgdrlsHERhqfQRDKE 661
Cdd:pfam13868 110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIleYLKEKAEREEERE------AER---EEIEE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1634229844 662 ATQELIEDLRKQLEHLQLLKLEAEQRRGRsssMGLQEYHSRARESELEQEVRRLKQdNRNLKEQNEE 728
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDELRAK---LYQEEQERKERQKEREEAEKKARQ-RQELQQAREE 243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
505-722 |
1.72e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 505 EDIADKVVFLERrVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSI 584
Cdd:COG4913 245 EDAREQIELLEP-IRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 585 EIENLQTRLQQLDEENselrsctpclkanIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQ 664
Cdd:COG4913 324 ELDELEAQIRGNGGDR-------------LEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1634229844 665 ELIEDLRKQLEHLQLLKLEAEQRRGRsssmglqeyhSRARESELEQEVRRLKQDNRNL 722
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRD----------LRRELRELEAEIASLERRKSNI 438
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
514-738 |
2.01e-06 |
|
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: 50.81 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 514 LERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLcKMEReksiEIENLQTRL 593
Cdd:pfam15558 85 REKQVIEKESRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQ-LQER----LEEACHKRQ 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 594 QQLDEENSELRSCTPCLKANIERL---------EEEKQKLLdeieSLTLRLSEEQEN-----KRR---MGDRLSHERHQF 656
Cdd:pfam15558 160 LKEREEQKKVQENNLSELLNHQARkvlvdcqakAEELLRRL----SLEQSLQRSQENyeqlvEERhreLREKAQKEEEQF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 657 QRDKEATQeliEDLRKQLEHLQLLKLEAEQRRGRS---SSMGLQEYHSRARESELEQEvrRLKQDNRNLKEQNEELNGQI 733
Cdd:pfam15558 236 QRAKWRAE---EKEEERQEHKEALAELADRKIQQArqvAHKTVQDKAQRARELNLERE--KNHHILKLKVEKEEKCHREG 310
|
....*
gi 1634229844 734 ITLSI 738
Cdd:pfam15558 311 IKEAI 315
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
489-783 |
2.09e-06 |
|
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: 51.56 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 489 MEALEDPSPELMEGPEEDIADKVVFLERrVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQL--KEQELRAcemvLE 566
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTE-IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlnIQKNIDK----IK 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 567 ETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELrsctpclKANIERLEEEKQKLLDEIES----LTLRLSEEQENK 642
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQL-------KDNIEKKQQEINEKTTEISNtqtqLNQLKDEQNKIK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 643 RRMGDRlsherhqfQRDKEATQELIEDLRKQLEHL--QLLKLEAEQRRGRSSSMG---------LQEYHSRARE-----S 706
Cdd:TIGR04523 267 KQLSEK--------QKELEQNNKKIKELEKQLNQLksEISDLNNQKEQDWNKELKselknqekkLEEIQNQISQnnkiiS 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 707 ELEQEVRRLKQ-------DNRNLKEQNEELNGQIITLSIQGAKSLFStafSESLAAEISsvsrdELMEAIQKQEEINFRL 779
Cdd:TIGR04523 339 QLNEQISQLKKeltnsesENSEKQRELEEKQNEIEKLKKENQSYKQE---IKNLESQIN-----DLESKIQNQEKLNQQK 410
|
....
gi 1634229844 780 QDYI 783
Cdd:TIGR04523 411 DEQI 414
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
512-729 |
2.22e-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: 51.33 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 512 VFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRA---------CEMVLE--ETRRQKELLCKMER 580
Cdd:pfam01576 127 VTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAkslsklknkHEAMISdlEERLKKEEKGRQEL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 581 EKSieIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDK 660
Cdd:pfam01576 207 EKA--KRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESER 284
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 661 EAtQELIEDLRKQL-EHLQLLKLEAEQRRGrsSSMGLQEYHSRaRESELEQEVRRLKQDNRNLKEQNEEL 729
Cdd:pfam01576 285 AA-RNKAEKQRRDLgEELEALKTELEDTLD--TTAAQQELRSK-REQEVTELKKALEEETRSHEAQLQEM 350
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
443-739 |
2.34e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.51 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 443 CSQCHKQINRLEDLSARLSDL--EMNSPTKRLSSKKVARYLHQSGALTMEALEDPSPELMEG---PEEDIADkvvfLERR 517
Cdd:TIGR00618 527 TRRMQRGEQTYAQLETSEEDVyhQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNlqnITVRLQD----LTEK 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 518 VLELEKDTAatGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETrrQKELLCKMEREKSI-----EIENLQTR 592
Cdd:TIGR00618 603 LSEAEDMLA--CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL--QLTLTQERVREHALsirvlPKELLASR 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 593 LQQLDEENSELRSCTPCLkaniERLeEEKQKLLDEIESLTLRLSEEQEnkrrmgdRLSHERHQFQRDKEATQELIEDLRK 672
Cdd:TIGR00618 679 QLALQKMQSEKEQLTYWK----EML-AQCQTLLRELETHIEEYDREFN-------EIENASSSLGSDLAAREDALNQSLK 746
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1634229844 673 QLEHLQLLKL----EAEQRRGRSSSMGLQeyhsrareseLEQEVRRLKQDNRNLKEQNEELNGQIITLSIQ 739
Cdd:TIGR00618 747 ELMHQARTVLkartEAHFNNNEEVTAALQ----------TGAELSHLAAEIQFFNRLREEDTHLLKTLEAE 807
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
498-799 |
2.80e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 498 ELMEGPEEDIADKVvfleRRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCK 577
Cdd:PTZ00121 1538 EAKKAEEKKKADEL----KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 578 MEREKSIEIENLQtrlqqldeENSELRSCTPCLKanieRLEEEKQKLLDEIESltlrlsEEQENKRRMGDRLSHERHQFQ 657
Cdd:PTZ00121 1614 KAEEAKIKAEELK--------KAEEEKKKVEQLK----KKEAEEKKKAEELKK------AEEENKIKAAEEAKKAEEDKK 1675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 658 RDKEATQELiEDLRKQLEhlQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLS 737
Cdd:PTZ00121 1676 KAEEAKKAE-EDEKKAAE--ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1634229844 738 IQGAKSLFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQdyIDRIIVAIMETNPSILE 799
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME--VDKKIKDIFDNFANIIE 1812
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
555-776 |
3.17e-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: 50.88 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 555 EQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSEL-------------------RSCTPCLKANIE 615
Cdd:pfam05483 98 EAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLikennatrhlcnllketcaRSAEKTKKYEYE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 616 RlEEEKQKLLD---EIESLTLRLSE---EQENKR-RMGDRLSHERHQFQRDKEATQELIEDLRKQLEhLQLLKLEAEQRR 688
Cdd:pfam05483 178 R-EETRQVYMDlnnNIEKMILAFEElrvQAENARlEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVS-LLLIQITEKENK 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 689 GRSSSMGLQEyhSRARESELEQEVRRLKQDNRNLKEQNEELNGQI--ITLSIQGAKSLfSTAFSESLaaEISSVSRDELM 766
Cdd:pfam05483 256 MKDLTFLLEE--SRDKANQLEEKTKLQDENLKELIEKKDHLTKELedIKMSLQRSMST-QKALEEDL--QIATKTICQLT 330
|
250
....*....|.
gi 1634229844 767 EAIQKQ-EEIN 776
Cdd:pfam05483 331 EEKEAQmEELN 341
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
509-717 |
4.00e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 50.74 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 509 DKVVFLERRVLELEKDTAATGEQHSRLRQEnLQLVHRANALEEQLKE-----QELRACEMVLEETRRQKELLCKMER--- 580
Cdd:TIGR00618 219 ERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQlrariEELRAQEAVLEETQERINRARKAAPlaa 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 581 -EKSIE-----IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKL--LDEIESLTLRLSEEQENKRRMGDR---L 649
Cdd:TIGR00618 298 hIKAVTqieqqAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLqtLHSQEIHIRDAHEVATSIREISCQqhtL 377
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1634229844 650 SHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRAREsELEQEVRRLKQ 717
Cdd:TIGR00618 378 TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ-ELQQRYAELCA 444
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
515-801 |
4.22e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 515 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKE-----QELRACEMVLEETRRQKELLCKMEREKSI-EIEN 588
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEElreleEELEELEAELAELQEELEELLEQLSLATEeELQD 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 589 LQTRLQQLDEENSELRsctpclkANIERLEEEKQKLLDEIESLTLRLSEEQENKRR------------------MGDRLS 650
Cdd:COG4717 197 LAEELEELQQRLAELE-------EELEEAQEELEELEEELEQLENELEAAALEERLkearlllliaaallallgLGGSLL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 651 HERHQ---------------FQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRL 715
Cdd:COG4717 270 SLILTiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 716 KQDNRNLKEQNEELNgqiITLSIQGAKSLFSTAFSESLAAEISSVSR-DELMEAIQKQEEINFRLQDYIDRIIVAIMETN 794
Cdd:COG4717 350 QELLREAEELEEELQ---LEELEQEIAALLAEAGVEDEEELRAALEQaEEYQELKEELEELEEQLEELLGELEELLEALD 426
|
....*..
gi 1634229844 795 PSILEVK 801
Cdd:COG4717 427 EEELEEE 433
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
537-733 |
4.83e-06 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 50.04 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 537 QENLQLVHRANaleEQLKEQELRACEMVLEETRRQKELLCKMereksieienlqtRLQQLDEenselrsctpclkanIER 616
Cdd:pfam10168 531 QECLQLLSRAT---QVFREEYLKKHDLAREEIQKRVKLLKLQ-------------KEQQLQE---------------LQS 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 617 LEEEKQKLLDEIESLTLRLSEEQENK----RRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRgrsS 692
Cdd:pfam10168 580 LEEERKSLSERAEKLAEKYEEIKDKQeklmRRCKKVLQRLNSQLPVLSDAEREMKKELETINEQLKHLANAIKQAK---K 656
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1634229844 693 SMGLQEYHSRARESELEQEVRRLKQDNR-----NLKEQNEELNGQI 733
Cdd:pfam10168 657 KMNYQRYQIAKSQSIRKKSSLSLSEKQRktikeILKQLGSEIDELI 702
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
471-687 |
7.38e-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: 49.56 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 471 RLSSKKVARYLHQSGALTMEALEDPSPELMEGPEEDIADKVVF----LERRVLELEKDTAATGEQHsRLRQENLQlvhRA 546
Cdd:pfam15709 296 RSSPTQTFVVTGNMESEEERSEEDPSKALLEKREQEKASRDRLraerAEMRRLEVERKRREQEEQR-RLQQEQLE---RA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 547 NALEEQLK-EQELRACEMVL------------EETRRQKELLCKMEREKS-IEIENLQTRLQQLDEENSElrsctpclkA 612
Cdd:pfam15709 372 EKMREELElEQQRRFEEIRLrkqrleeerqrqEEEERKQRLQLQAAQERArQQQEEFRRKLQELQRKKQQ---------E 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1634229844 613 NIERLEEEKQKLldeiESLTLRLSEEQenKRRMG----DRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQR 687
Cdd:pfam15709 443 EAERAEAEKQRQ----KELEMQLAEEQ--KRLMEmaeeERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQ 515
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
515-728 |
8.58e-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: 48.76 E-value: 8.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 515 ERRVLELEKDtaatgEQHSRLRQENLQLVHRANALEEQLKEQE----LRACEMVLEETRRQKELLCKMEREKSIEIENLQ 590
Cdd:pfam13868 87 QKRQEEYEEK-----LQEREQMDEIVERIQEEDQAEAEEKLEKqrqlREEIDEFNEEQAEWKELEKEEEREEDERILEYL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 591 TRLQQLDEEnselrsctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQF---QRDKEAT---- 663
Cdd:pfam13868 162 KEKAEREEE----------REAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERkerQKEREEAekka 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 664 ---QELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDN--RNLKEQNEE 728
Cdd:pfam13868 232 rqrQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEhrRELEKQIEE 301
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
515-627 |
1.13e-05 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 47.07 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 515 ERRVLELEKDTAATGEQHSR-LRQENLQLVHRANALEEQLKEQELR-ACEMVLEETRRQKELL------CKMEREKSIEI 586
Cdd:pfam14988 84 EREIQDLEEEKEKVRAETAEkDREAHLQFLKEKALLEKQLQELRILeLGERATRELKRKAQALklaakqALSEFCRSIKR 163
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1634229844 587 EN--LQTRLQQLDEEnselrscTPCLKANIERLEEEKQKLLDE 627
Cdd:pfam14988 164 ENrqLQKELLQLIQE-------TQALEAIKSKLENRKQRLKEE 199
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
3-223 |
1.43e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 48.83 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 3 SAPPASPPGSEPPGPDPEPGGPDGPGAAQLAPGPAELRLGAPVGGPDPQSPGLDEPAPGAAADGGARWSAGPAPGLEGGP 82
Cdd:PRK07764 591 APGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWP 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 83 RDPGPSAPPPRSGPRGQLASPDAPGPGPRSEAPLPeldplfSWTEEPEecgPASCPESAPfRLQGSSSSHRARGEVDVFS 162
Cdd:PRK07764 671 AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAP------AATPPAG---QADDPAAQP-PQAAQGASAPSPAADDPVP 740
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1634229844 163 PFPAPTAGELALEQGPGSPPQPSDLSQTHPLPSEPVGSQEDGPRLRAvfDALDGDGDGFVR 223
Cdd:PRK07764 741 LPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAE--DDAPSMDDEDRR 799
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
505-800 |
1.63e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 505 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRacemvLEETRRQKELLCKMEREKSI 584
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE-----LAQAQEELESLQEEAEELQE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 585 EIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQ 664
Cdd:COG4372 116 ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 665 ELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARES---ELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGA 741
Cdd:COG4372 196 AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAlldALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1634229844 742 KSLFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRIIVAIMETNPSILEV 800
Cdd:COG4372 276 EELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
530-718 |
1.82e-05 |
|
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: 48.50 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 530 EQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLC--KMEREKSIEIENLQTRLQQLDEENSELRSCT 607
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESsrEIVKSYENELDPLKNRLKEIEHNLSKIMKLD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 608 PCLKAnIERLEEEKQKLLDEIESLTLR--------LSEEQENKRRMGDRLSHERHQFQRDkeatqelIEDLRKQLEHLQL 679
Cdd:TIGR00606 269 NEIKA-LKSRKKQMEKDNSELELKMEKvfqgtdeqLNDLYHNHQRTVREKERELVDCQRE-------LEKLNKERRLLNQ 340
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1634229844 680 LKLEAEQRRGRSS-SMGLQEYHSRARESELEQEVRRLKQD 718
Cdd:TIGR00606 341 EKTELLVEQGRLQlQADRHQEHIRARDSLIQSLATRLELD 380
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
538-681 |
1.84e-05 |
|
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: 47.32 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 538 ENLQLVHRANAL----EEQLKE--QELRACEMVLEETRRQ-KELLCKMEREKSIEIENLQTRLQQLDEENSELRSctpcl 610
Cdd:smart00787 151 ENLEGLKEDYKLlmkeLELLNSikPKLRDRKDALEEELRQlKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVK----- 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1634229844 611 kaNIERLEEEKQKLLDEIESLTLRLSEEQenkrrmgDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLK 681
Cdd:smart00787 226 --KLEELEEELQELESKIEDLTNKKSELN-------TEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
498-638 |
2.16e-05 |
|
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: 46.46 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 498 ELMEGPEE--DIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKE----QELRACEMVLEETRRQ 571
Cdd:COG1579 25 RLKELPAElaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnKEYEALQKEIESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1634229844 572 KELLCKMEREKSIEIENLQTRLQ----QLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEE 638
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAeleaELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
614-793 |
2.53e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 614 IERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSH----ERHQFQR-DKEATQELIEDLRKQLEHL-----QLLKLE 683
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlAEYSWDEiDVASAEREIAELEAELERLdassdDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 684 AEQRRgrsssmglqeyhSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLS------IQGAKSLFSTAFSESLAAEI 757
Cdd:COG4913 692 EQLEE------------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQdrleaaEDLARLELRALLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|....*.
gi 1634229844 758 SSVSRDELMEAIQKQEEINFRLQDYIDRIIVAIMET 793
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
450-716 |
2.53e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 450 INRLEDLSARLSDLEM--NSPTKRLSSKKVARYL----HQSGALTMEALEDPSPELmegpeEDIADKVVFLERRVLELEK 523
Cdd:PRK03918 472 EEKERKLRKELRELEKvlKKESELIKLKELAEQLkeleEKLKKYNLEELEKKAEEY-----EKLKEKLIKLKGEIKSLKK 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 524 DTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELlcKMEREKSIEIENLQTRLQQLDEENSEL 603
Cdd:PRK03918 547 ELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKEL--EPFYNEYLELKDAEKELEREEKELKKL 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 604 RSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQ-ENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKL 682
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
250 260 270
....*....|....*....|....*....|....
gi 1634229844 683 EAEQRRGRSSSMGlqeyHSRARESELEQEVRRLK 716
Cdd:PRK03918 705 EREKAKKELEKLE----KALERVEELREKVKKYK 734
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
489-736 |
2.89e-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: 47.81 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 489 MEALEDPSPELMEGPEEDIADKVvflERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQE-LRACEMV-LE 566
Cdd:pfam15921 247 LEALKSESQNKIELLLQQHQDRI---EQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNsMYMRQLSdLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 567 ETRRQ-KELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRM 645
Cdd:pfam15921 324 STVSQlRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 646 GDRlsherhqfqrdKEATQELIEDLRKQLE--HLQLLKLEAEQRRGRSSSMGLQEYHSRA---RESELEQE---VRRLKQ 717
Cdd:pfam15921 404 WDR-----------DTGNSITIDHLRRELDdrNMEVQRLEALLKAMKSECQGQMERQMAAiqgKNESLEKVsslTAQLES 472
|
250
....*....|....*....
gi 1634229844 718 DNRNLKEQNEELNGQIITL 736
Cdd:pfam15921 473 TKEMLRKVVEELTAKKMTL 491
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
585-733 |
2.94e-05 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 44.17 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 585 EIENLQTRLQQLDEEnselrsctpclkanIERLEEEKQKLLDEIESLTLRLSEEQENKRRmgdrlsherhQFQRDKEATQ 664
Cdd:pfam07926 2 ELSSLQSEIKRLKEE--------------AADAEAQLQKLQEDLEKQAEIAREAQQNYER----------ELVLHAEDIK 57
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1634229844 665 ELiEDLRKQLEHLQL----LKLEAEQRRgrsSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQI 733
Cdd:pfam07926 58 AL-QALREELNELKAeiaeLKAEAESAK---AELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQL 126
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
505-736 |
3.56e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 505 EDIADKVVFLERRVLELEKDTAATGEQHSRLrqenlqlvhranaleEQLKEQELRacemvLEETRRQKELLCKMEREKSI 584
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLERA---------------EDLVEAEDR-----IERLEERREDLEELIAERRE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 585 EIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLseeQENKRRMgDRLSHERHQFQRDKEATQ 664
Cdd:PRK02224 531 TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL---AELKERI-ESLERIRTLLAAIADAED 606
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1634229844 665 ElIEDLRKQLEHLQLLKleaEQRRGRsssmgLQEyhSRARESELEQE-----VRRLKQDNRNLKEQNEELNGQIITL 736
Cdd:PRK02224 607 E-IERLREKREALAELN---DERRER-----LAE--KRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDEL 672
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
541-690 |
4.21e-05 |
|
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: 45.69 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 541 QLVHRANALEEQLK--EQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEE-------------NSELRS 605
Cdd:COG1579 21 RLEHRLKELPAELAelEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyealQKEIES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 606 ctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHL------QL 679
Cdd:COG1579 101 ----LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELaakippEL 176
|
170
....*....|.
gi 1634229844 680 LKLEAEQRRGR 690
Cdd:COG1579 177 LALYERIRKRK 187
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
514-727 |
4.77e-05 |
|
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: 47.04 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 514 LERRVLELEKdtaatgEQHSRLRQENLQL-VHRANALEeQLKEQELRACEMV---LEETRRQKELlckmEREKSIEIENL 589
Cdd:pfam17380 350 LERIRQEERK------RELERIRQEEIAMeISRMRELE-RLQMERQQKNERVrqeLEAARKVKIL----EEERQRKIQQQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 590 QTRLQQLDEENSELRsctpclKANIERLEEEKQKLLDEIESLTL-------RLSEEQENKRRMGDRLSHERHQFQRDKEA 662
Cdd:pfam17380 419 KVEMEQIRAEQEEAR------QREVRRLEEERAREMERVRLEEQerqqqveRLRQQEEERKRKKLELEKEKRDRKRAEEQ 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1634229844 663 TQELIEdlrKQLEHLQLLKLEAEQRRgrssSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNE 727
Cdd:pfam17380 493 RRKILE---KELEERKQAMIEEERKR----KLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE 550
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
516-780 |
4.82e-05 |
|
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: 47.04 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 516 RRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLK-------------EQELRACEMVLEETRRQKELLCKMEREK 582
Cdd:pfam05557 72 REQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKnelselrrqiqraELELQSTNSELEELQERLDLLKAKASEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 583 SIEIENLQT----------RLQQLDEENSELRSCTPCLK------ANIERLEEEKQKLLDEIEsltlRLSEEQENKRRMG 646
Cdd:pfam05557 152 EQLRQNLEKqqsslaeaeqRIKELEFEIQSQEQDSEIVKnskselARIPELEKELERLREHNK----HLNENIENKLLLK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 647 DRLSHERHQFQRDKEATQELIeDLRKQLEHLQlLKLEAEQRRGRSSSMGLQeyhsraRESELEQEVRRLKQDNRNLKEQN 726
Cdd:pfam05557 228 EEVEDLKRKLEREEKYREEAA-TLELEKEKLE-QELQSWVKLAQDTGLNLR------SPEDLSRRIEQLQQREIVLKEEN 299
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1634229844 727 EELNGQIITLSIQGakslfstafsESLAAEISSVSRD--ELMEAIQKQEEINFRLQ 780
Cdd:pfam05557 300 SSLTSSARQLEKAR----------RELEQELAQYLKKieDLNKKLKRHKALVRRLQ 345
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
445-779 |
4.83e-05 |
|
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: 47.02 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 445 QCHKQINRLEDLSARLSDL-----EMNSPTKrLSSKKVARYLHQSGALTMEaLED------PSPELMEGPEED--IADKV 511
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESrdkanQLEEKTK-LQDENLKELIEKKDHLTKE-LEDikmslqRSMSTQKALEEDlqIATKT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 512 VFlerrvlELEKDTAATGEQHSRLRQENLQLVHRANA----LEEQLKEQELRacemvLEETRRQKELLCKMEREKSIEIE 587
Cdd:pfam05483 326 IC------QLTEEKEAQMEELNKAKAAHSFVVTEFEAttcsLEELLRTEQQR-----LEKNEDQLKIITMELQKKSSELE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 588 NLQTRLQQLDEENSELRsctpclkanieRLEEEKQKLLDEIESLTlRLSEEQENKRRMGDRLSHERHQFQRDKE------ 661
Cdd:pfam05483 395 EMTKFKNNKEVELEELK-----------KILAEDEKLLDEKKQFE-KIAEELKGKEQELIFLLQAREKEIHDLEiqltai 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 662 ATQE-----LIEDLRKQLEHLQLLKLEAEqrrGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITL 736
Cdd:pfam05483 463 KTSEehylkEVEDLKTELEKEKLKNIELT---AHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENL 539
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1634229844 737 SIQgakslfstafSESLAAEISSVsRDELmeaIQKQEEINFRL 779
Cdd:pfam05483 540 EEK----------EMNLRDELESV-REEF---IQKGDEVKCKL 568
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
206-264 |
5.16e-05 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 41.76 E-value: 5.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1634229844 206 RLRAVFDALDGDGDGFVRIEDFIQFATVYGAEQVKDLTKYL----DPSGLGVISFEDFYQGIT 264
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMirevDKDGDGKIDFEEFLELMA 63
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
514-718 |
5.71e-05 |
|
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: 46.71 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 514 LERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRacemvLEETRRQK-ELLCKMEREKSiEIENLQTR 592
Cdd:pfam01576 375 LEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQAR-----LSESERQRaELAEKLSKLQS-ELESVSSL 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 593 LQQLDEENS----ELRSCTPCLKANIERLEEE-KQKLL---------DEIESLTLRLSEEQENKRRMGDRLSHERHQFQR 658
Cdd:pfam01576 449 LNEAEGKNIklskDVSSLESQLQDTQELLQEEtRQKLNlstrlrqleDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSD 528
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1634229844 659 DKEATQELIEDLrKQLEhlqllklEAEQRRGRSSSMGLQEYHSRARESE-LEQEVRRLKQD 718
Cdd:pfam01576 529 MKKKLEEDAGTL-EALE-------EGKKRLQRELEALTQQLEEKAAAYDkLEKTKNRLQQE 581
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
542-717 |
7.20e-05 |
|
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: 46.48 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 542 LVHRANALEEQLKEQELRACEmvLEETRRQKELLCK---MEREKSIEIENLQTRLQQLDEENSE-LRSCtpclkanIERL 617
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQ--QQNAERLLEEFCQrigQQLDAAEELEELLAELEAQLEELEEqAAEA-------VEQR 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 618 EEEKQKLlDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQrrgrsssmglq 697
Cdd:COG3096 581 SELRQQL-EQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDE----------- 648
|
170 180
....*....|....*....|
gi 1634229844 698 eyhSRARESELEQEVRRLKQ 717
Cdd:COG3096 649 ---LAARKQALESQIERLSQ 665
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
612-786 |
9.54e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 612 ANIERLEEEKQKLLDEIESLTLRLSEEQ---ENKRRMGDRLSHERHQFQRDKEATQELIEdlRKQLEHL-QLLKLEAEQR 687
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDliiDEKRQQLERLRREREKAERYQALLKEKRE--YEGYELLkEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 688 RGRSSSMGLQEyHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKSLfstafsESLAAEISSVsRDELME 767
Cdd:TIGR02169 241 AIERQLASLEE-ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKI------GELEAEIASL-ERSIAE 312
|
170
....*....|....*....
gi 1634229844 768 AIQKQEEINFRLQDYIDRI 786
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEI 331
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
448-730 |
9.62e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 448 KQINRLEDLSARLSDLEMNSPTKRLSSKKVAR---YLHQSGALTMEALEDPspELMEGPE---------EDIADKVVFLE 515
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEArieELEEDLHKLEEALNDL--EARLSHSripeiqaelSKLEEEVSRIE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 516 RRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQE---------LRACEMVLEETRRQKELLCKMEREKSIEI 586
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEkeienlngkKEELEEELEELEAALRDLESRLGDLKKER 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 587 ENLQtrlqqldeenselrsctpclkANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQEL 666
Cdd:TIGR02169 892 DELE---------------------AQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE 950
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1634229844 667 --IEDLRKQLEhlqllKLEAEQRRGRSSSMG-LQEYH-SRARESELEQEVRRLKQDNRNLKEQNEELN 730
Cdd:TIGR02169 951 lsLEDVQAELQ-----RVEEEIRALEPVNMLaIQEYEeVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
516-725 |
9.82e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.97 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 516 RRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMERE---KSIEIENLQTR 592
Cdd:pfam10174 232 QTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQElskKESELLALQTK 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 593 LQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQ--------------ENK-------RRMGDRLS- 650
Cdd:pfam10174 312 LETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKEsflnkktkqlqdltEEKstlageiRDLKDMLDv 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 651 HER--HQFQRDKEATQELIEDLRKQLEHLQ----------------LLKLE---AEQRRGRSSsmgLQEYHSRARESELE 709
Cdd:pfam10174 392 KERkiNVLQKKIENLQEQLRDKDKQLAGLKervkslqtdssntdtaLTTLEealSEKERIIER---LKEQREREDRERLE 468
|
250
....*....|....*.
gi 1634229844 710 qEVRRLKQDNRNLKEQ 725
Cdd:pfam10174 469 -ELESLKKENKDLKEK 483
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
505-776 |
1.02e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 505 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEmvleETRRQKELLCKMEREKSI 584
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE----EKKKADELKKAEELKKAE 1561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 585 EIENLQTRLQQLDEENSELRsctpclKANIERLEEEKQklldeIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEAtq 664
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALR------KAEEAKKAEEAR-----IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-- 1628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 665 eliEDLRKQLEhlQLLKLEAEQRRgRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNgqiitlsiQGAKSL 744
Cdd:PTZ00121 1629 ---EEEKKKVE--QLKKKEAEEKK-KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK--------KAAEAL 1694
|
250 260 270
....*....|....*....|....*....|....
gi 1634229844 745 FSTAFSESLAAEISSVSRDELMEA--IQKQEEIN 776
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAeeLKKAEEEN 1728
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
545-739 |
1.10e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 545 RANALEEQLKEQELRAcEMVLEETRRQKEllcKMEREKSIEIEnlqtrlqqldEENSELRSctpclkanieRLEEEKQKL 624
Cdd:PRK12704 25 RKKIAEAKIKEAEEEA-KRILEEAKKEAE---AIKKEALLEAK----------EEIHKLRN----------EFEKELRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 625 LDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEyhsrAR 704
Cdd:PRK12704 81 RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEE----AK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1634229844 705 E---SELEQEVR-----RLKQDNRNLKEQNEELNGQIITLSIQ 739
Cdd:PRK12704 157 EillEKVEEEARheaavLIKEIEEEAKEEADKKAKEILAQAIQ 199
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
505-733 |
1.15e-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: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 505 EDIADKVVFLErrvLELEKDTAATGEQHSRlrqeNLQLVHRANALEEQLKE-QELRAcemvlEETR---------RQKE- 573
Cdd:pfam01576 429 AELAEKLSKLQ---SELESVSSLLNEAEGK----NIKLSKDVSSLESQLQDtQELLQ-----EETRqklnlstrlRQLEd 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 574 ----LLCKMEREKSIEiENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMgdrl 649
Cdd:pfam01576 497 ernsLQEQLEEEEEAK-RNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL---- 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 650 sherhqfQRDKEATQELIEDLRKQLEHLQLL--KLEAEQRR-------GRSSSMGLQEYHSRARESELEQEVRRLK---- 716
Cdd:pfam01576 572 -------EKTKNRLQQELDDLLVDLDHQRQLvsNLEKKQKKfdqmlaeEKAISARYAEERDRAEAEAREKETRALSlara 644
|
250
....*....|....*...
gi 1634229844 717 -QDNRNLKEQNEELNGQI 733
Cdd:pfam01576 645 lEEALEAKEELERTNKQL 662
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
504-686 |
1.34e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 43.90 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 504 EEDIADKVVFLERRVLELEKDtaatgeqHSRLRQENLQLVHRANALEEQLKEQELRACEmvLEEtrRQKELLCKME---- 579
Cdd:pfam04012 17 LDKAEDPEKMLEQAIRDMQSE-------LVKARQALAQTIARQKQLERRLEQQTEQAKK--LEE--KAQAALTKGNeela 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 580 REKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLE-------EEKQKLLDEIESLTLRlseEQENKRRMGDRLSHE 652
Cdd:pfam04012 86 REALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALEtkiqqlkAKKNLLKARLKAAKAQ---EAVQTSLGSLSTSSA 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 1634229844 653 RHQFQR--DKEATQELIEDLRKQLEHLQLLKLEAEQ 686
Cdd:pfam04012 163 TDSFERieEKIEEREARADAAAELASAVDLDAKLEQ 198
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
532-729 |
1.43e-04 |
|
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.
Pssm-ID: 405365 [Multi-domain] Cd Length: 191 Bit Score: 43.63 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 532 HSRLRQENLQLvhraNALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLqqldEENSELRSCTPcLK 611
Cdd:pfam14662 17 NQKLLQENSKL----KATVETREETNAKLLEENLNLRKQAKSQQQAVQKEKLLEEELEDLKL----IVNSLEEARRS-LL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 612 ANIERLEEEKQKLLDEIESLtlrlseEQENKRrmgdrLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRS 691
Cdd:pfam14662 88 AQNKQLEKENQSLLQEIESL------QEENKK-----NQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEK 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 1634229844 692 SSMGLQEYHSRARESELEQEvrrLKQDNRNLKEQNEEL 729
Cdd:pfam14662 157 TTQIEELKSTVEEYSSIEEE---LRAEKSRLESQLPDM 191
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
536-737 |
1.53e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 536 RQENLQLVHRANALEEQLKE--QELRACEMVLEETRRQKEllckmerEKSIEIENLQTRLQQLDEENSELRSctpcLKAN 613
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAEldEEIERYEEQREQARETRD-------EADEVLEEHEERREELETLEAEIED----LRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 614 IERLEEEKQKLLDEIESLTLRLSE-EQENKRRMGD---------RLSHERHQFQRDKEATQELIEDLRKQLehlQLLKLE 683
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEElEEERDDLLAEaglddadaeAVEARREELEDRDEELRDRLEECRVAA---QAHNEE 343
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1634229844 684 AEQRRGRSSSmgLQEYHSRARE--SELEQEVRRLKQDNRNLKEQNEELNGQIITLS 737
Cdd:PRK02224 344 AESLREDADD--LEERAEELREeaAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
580-787 |
1.57e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.33 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 580 REKSIEIENLQTRLQQLDEENSELRSCTPCLKAN-IERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERhQFQR 658
Cdd:COG5185 242 ESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAEsSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEE-QLAA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 659 dKEATQELIEDLRKQLEHLQLLKLEAEQRRgRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSI 738
Cdd:COG5185 321 -AEAEQELEESKRETETGIQNLTAEIEQGQ-ESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQ 398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1634229844 739 QGAKSLFStaFSESLAAEISSVSRD--ELMEAIQKQEEINFRLQDYIDRII 787
Cdd:COG5185 399 NQRGYAQE--ILATLEDTLKAADRQieELQRQIEQATSSNEEVSKLLNELI 447
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
536-730 |
1.62e-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: 45.49 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 536 RQENLQLVHRANALEEQLKE------QELRACEMVLEETRRQKELLCK--MEREKSIEIEN-----LQTR-------LQQ 595
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEmlrkvvEELTAKKMTLESSERTVSDLTAslQEKERAIEATNaeitkLRSRvdlklqeLQH 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 596 LDEENSELRSC-TPCLKANIERLEEEK--QKLLDEIESLTLRLSEEQenkrRMGDRLSHERHQFQRDkeatqelIEDLRK 672
Cdd:pfam15921 536 LKNEGDHLRNVqTECEALKLQMAEKDKviEILRQQIENMTQLVGQHG----RTAGAMQVEKAQLEKE-------INDRRL 604
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1634229844 673 QLEHLQLLKLEAEQR----RGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNL----KEQNEELN 730
Cdd:pfam15921 605 ELQEFKILKDKKDAKirelEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLlnevKTSRNELN 670
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
76-205 |
1.79e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 45.25 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 76 PGLEGGPRDPGPSAPPPRSGPRGQLASPDAPGPGPRSEAPLPELDPLFSWTEEPEECGPASCPESAPFRLQGSSSSHRAR 155
Cdd:PRK12323 365 PGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGP 444
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1634229844 156 GEVD--VFSPFPAPTAGELALEQGPGSPPQPSDLSQTHPLPSEPVGSQEDGP 205
Cdd:PRK12323 445 GGAPapAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDP 496
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
562-688 |
1.86e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 562 EMVLEETRRqkELLCKMEREKSIEIENLQTRLQQLDEENSELRSctpclkaNIERLEEEKQKLLDEIESLTLRLSEEQEN 641
Cdd:COG2433 379 EEALEELIE--KELPEEEPEAEREKEHEERELTEEEEEIRRLEE-------QVERLEAEVEELEAELEEKDERIERLERE 449
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1634229844 642 KRRMGDRlshERHQFQRDKEAT--QELIEDLRKQLEHLQ--LLKLEAEQRR 688
Cdd:COG2433 450 LSEARSE---ERREIRKDREISrlDREIERLERELEEERerIEELKRKLER 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
519-722 |
1.95e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 519 LELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQldE 598
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG--E 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 599 ENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQ 678
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1634229844 679 LLKLEAEQR-RGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNL 722
Cdd:COG1196 735 EELLEELLEeEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
82-243 |
1.95e-04 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 44.08 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 82 PRDPGPSAPPPRsgPRGQLASPDAPGPGPRSEAPLPELDPLFSWTEEPeecgPASCPESAPFRLQGSSSSHRARGEVDVF 161
Cdd:PHA02682 81 PLAPSPACAAPA--PACPACAPAAPAPAVTCPAPAPACPPATAPTCPP----PAVCPAPARPAPACPPSTRQCPPAPPLP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 162 SPFPAPTAGELALEQGPGSPPQPSDLSQThpLPSEPVGSQEDGPRLRAvfDALDGDGDGfvriEDFIQFATVYGAEQVKD 241
Cdd:PHA02682 155 TPKPAPAAKPIFLHNQLPPPDYPAASCPT--IETAPAASPVLEPRIPD--KIIDADNDD----KDLIKKELADIADSVRD 226
|
..
gi 1634229844 242 LT 243
Cdd:PHA02682 227 LN 228
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
514-725 |
2.25e-04 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 44.25 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 514 LERRVLELEKDTAATGEQHSRLRQEN------LQLVhrANALEEQLKEQElraCEmvlEETRRQKELLckmEREKSIEIE 587
Cdd:pfam04849 99 LTERNEALEEQLGSAREEILQLRHELskkddlLQIY--SNDAEESETESS---CS---TPLRRNESFS---SLHGCVQLD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 588 NLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKL-LDEIESLTL------RLSEEQENKRRmgdrlSHERHQfqrdK 660
Cdd:pfam04849 168 ALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLmSDCVEQLSEanqqmaELSEELARKME-----ENLRQQ----E 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1634229844 661 EATQEL--IEDLRKQL-------EHLQLLkLEAEQRRGRSSSMGLQEYhsRARESELEQEVRRLKQDNRNLKEQ 725
Cdd:pfam04849 239 EITSLLaqIVDLQHKCkelgienEELQQH-LQASKEAQRQLTSELQEL--QDRYAECLGMLHEAQEELKELRKK 309
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
549-733 |
2.46e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 44.46 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 549 LEEQLK--EQELRACEMVLEETRRQKELLCKMEReksieieNLQTRLQQLDEENSELRSctpclkaNIERLEEEKQKLLD 626
Cdd:pfam09726 400 LEQDIKklKAELQASRQTEQELRSQISSLTSLER-------SLKSELGQLRQENDLLQT-------KLHNAVSAKQKDKQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 627 EIESLTLRLSEEQENKRRMGDRLSHERhQFQRDKEATQEliedlrkqlehlQLLKLEAEQRRGRSSSMglqeyhsRARES 706
Cdd:pfam09726 466 TVQQLEKRLKAEQEARASAEKQLAEEK-KRKKEEEATAA------------RAVALAAASRGECTESL-------KQRKR 525
|
170 180
....*....|....*....|....*..
gi 1634229844 707 ELEQEVRRLKQDNRNLKEQNEELNGQI 733
Cdd:pfam09726 526 ELESEIKKLTHDIKLKEEQIRELEIKV 552
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
452-789 |
2.51e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 452 RLEDLSARLSDLEMNSPTKRLSSKKVARYLHQsgaltMEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTAATGEQ 531
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEE-----LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 532 HSRLRQE--NLQLVHRANALEEQLKEQE-------------------------------LRACEMVLEETRRQKEllcKM 578
Cdd:COG4717 222 LEELEEEleQLENELEAAALEERLKEARlllliaaallallglggsllsliltiagvlfLVLGLLALLFLLLARE---KA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 579 EREKSIEIENLQTRLQQLDEEnsELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMgDRLSHERHQFQR 658
Cdd:COG4717 299 SLGKEAEELQALPALEELEEE--ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL-QLEELEQEIAAL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 659 DKEATQELIEDLRKQLEHLQ-LLKLEAE----QRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQI 733
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEeYQELKEEleelEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL 455
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1634229844 734 ITLSiqgakslfstafseslaAEISSVSRD-ELMEAIQKQEEINFRLQDYIDRIIVA 789
Cdd:COG4717 456 AELE-----------------AELEQLEEDgELAELLQELEELKAELRELAEEWAAL 495
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
562-786 |
3.00e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 562 EMVLEETRRQKELLcKMEREKSIE-----IENLQTRLQQLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLS 636
Cdd:COG1340 7 SSSLEELEEKIEEL-REEIEELKEkrdelNEELKELAEKRDELNAQVKE----LREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 637 EEQENKRRMGDRLshERHQFQRDKEATQEL-IEDLRKQLEHL------QLLKLEAEQRR-GRSSSMGlQEYHSRARESEL 708
Cdd:COG1340 82 ELNEKLNELREEL--DELRKELAELNKAGGsIDKLRKEIERLewrqqtEVLSPEEEKELvEKIKELE-KELEKAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 709 EQEVRRLKQDNRNLKEQNEELNGQIITLS--IQGAKSLFSTAFSEslaaeissvsRDELM-EAIQKQEEINfRLQDYIDR 785
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKELAeeAQELHEEMIELYKE----------ADELRkEADELHKEIV-EAQEKADE 227
|
.
gi 1634229844 786 I 786
Cdd:COG1340 228 L 228
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
453-774 |
3.23e-04 |
|
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: 44.56 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 453 LEDLSARLSDLEM--NSPTKRLS--------SKKVARYLHQSGALTmEALEDPSPELMEGPEEdiadkvvflerrVLELE 522
Cdd:COG3096 315 LEELSARESDLEQdyQAASDHLNlvqtalrqQEKIERYQEDLEELT-ERLEEQEEVVEEAAEQ------------LAEAE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 523 KDTAATGEQHSRLRQenlQLVHRANALEEQLK-----EQELRAcemvLEETRRqkelLCKMErekSIEIEN-------LQ 590
Cdd:COG3096 382 ARLEAAEEEVDSLKS---QLADYQQALDVQQTraiqyQQAVQA----LEKARA----LCGLP---DLTPENaedylaaFR 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 591 TRLQQLDEENSELR---SCTPCLKANIERLEEEKQKLLDEIESltlrlSEEQENKRRMGDRLSHERHQFQRDKEATQELI 667
Cdd:COG3096 448 AKEQQATEEVLELEqklSVADAARRQFEKAYELVCKIAGEVER-----SQAWQTARELLRRYRSQQALAQRLQQLRAQLA 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 668 E---DLRKQLEHLQLLKlEAEQRRGR--SSSMGLQEYHSR--ARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQG 740
Cdd:COG3096 523 EleqRLRQQQNAERLLE-EFCQRIGQqlDAAEELEELLAEleAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARA 601
|
330 340 350
....*....|....*....|....*....|....*.
gi 1634229844 741 AKSLFSTAFSESLAAEI--SSVSRDELMEAIQKQEE 774
Cdd:COG3096 602 PAWLAAQDALERLREQSgeALADSQEVTAAMQQLLE 637
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
589-736 |
3.41e-04 |
|
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: 42.99 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 589 LQTRLQQLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEA-----T 663
Cdd:COG1579 12 LQELDSELDRLEHRLKE----LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1634229844 664 QELIEDLRKQLEHLQLLKLEAEQRRgrsssMGLQEYHSRAR------ESELEQEVRRLKQDNRNLKEQNEELNGQIITL 736
Cdd:COG1579 88 NKEYEALQKEIESLKRRISDLEDEI-----LELMERIEELEeelaelEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
509-733 |
3.45e-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: 44.12 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 509 DKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLK--EQELRACEMVLEETRRQKELLCKMEREKSIEI 586
Cdd:pfam07888 94 EKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKtlTQRVLERETELERMKERAKKAGAQRKEEEAER 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 587 ENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQ----ENKRRMGD-RLSHER-HQFQRDK 660
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHrkeaENEALLEElRSLQERlNASERKV 253
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1634229844 661 EATQELIEDLRKQLEH----LQLLKLEAEQRRGRSSSMGLQEYHSRARESeleQEVRRLKQDNRNLKEQNEELNGQI 733
Cdd:pfam07888 254 EGLGEELSSMAAQRDRtqaeLHQARLQAAQLTLQLADASLALREGRARWA---QERETLQQSAEADKDRIEKLSAEL 327
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
511-676 |
3.49e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 511 VVFLERRVLELEkdtaatgEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKEllckmerEKSIEIENLQ 590
Cdd:PRK12705 22 VVLLKKRQRLAK-------EAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE-------ELQREEERLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 591 TRLQQLDEENselrsctpclkaniERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLshERHQFQRDKEATQELIEDL 670
Cdd:PRK12705 88 QKEEQLDARA--------------EKLDNLENQLEEREKALSARELELEELEKQLDNEL--YRVAGLTPEQARKLLLKLL 151
|
....*.
gi 1634229844 671 RKQLEH 676
Cdd:PRK12705 152 DAELEE 157
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
541-729 |
3.98e-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: 43.37 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 541 QLVHRaNALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCtpclkaNIERLEEE 620
Cdd:pfam13868 27 QIAEK-KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQE------EYEEKLQE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 621 KQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELiEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYH 700
Cdd:pfam13868 100 REQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKEL-EKEEEREEDERILEYLKEKAEREEEREAEREEI 178
|
170 180
....*....|....*....|....*....
gi 1634229844 701 SRARESELeQEVRRLKQDNRNLKEQNEEL 729
Cdd:pfam13868 179 EEEKEREI-ARLRAQQEKAQDEKAERDEL 206
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
447-685 |
4.06e-04 |
|
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: 44.19 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 447 HKQINRLEDLSARLSDLEMN----SPTKRLSSKKVARYLHQSGALTMEALEDPSPELMEGPEEDIADKVVFLERRVLELE 522
Cdd:pfam02463 757 LKKEEKEEEKSELSLKEKELaeerEKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELE 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 523 KDTAATGEQHSR--LRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEEN 600
Cdd:pfam02463 837 ELALELKEEQKLekLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKE 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 601 SELRSCTPCLKANIERLEEEKQKLLDEIESL-----TLRLSEEQENKrRMGDRLSHERhqFQRDKEATQELIEDLRKQLE 675
Cdd:pfam02463 917 NEIEERIKEEAEILLKYEEEPEELLLEEADEkekeeNNKEEEEERNK-RLLLAKEELG--KVNLMAIEEFEEKEERYNKD 993
|
250
....*....|
gi 1634229844 676 HLQLLKLEAE 685
Cdd:pfam02463 994 ELEKERLEEE 1003
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
456-781 |
4.14e-04 |
|
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: 44.06 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 456 LSARLSDLEMNSPTKRLSSKKVARYLHQSGALtmEALEDPSPELmEGPEEDiadkvvFLERRVLELEkdtaatgeqhsrl 535
Cdd:pfam12128 202 IVAILEDDGVVPPKSRLNRQQVEHWIRDIQAI--AGIMKIRPEF-TKLQQE------FNTLESAELR------------- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 536 rqenLQLVHRANALEEQLKEQELRACEmvlEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSctpclkaNIE 615
Cdd:pfam12128 260 ----LSHLHFGYKSDETLIASRQEERQ---ETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRS-------ELE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 616 RLEEEKQKLLDE-IEslTLRLSEEQENKRRMGDRLSHERHQFQRDK-----EATQELI----EDLRKQLEHLQllKLEAE 685
Cdd:pfam12128 326 ALEDQHGAFLDAdIE--TAAADQEQLPSWQSELENLEERLKALTGKhqdvtAKYNRRRskikEQNNRDIAGIK--DKLAK 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 686 QRRGRSSSMGLQEYHSRARESELEQEvrrLKQDNRNLKEQNEELNGQIITLSIQGAKSLFSTAFSESLAAEISSVSR-DE 764
Cdd:pfam12128 402 IREARDRQLAVAEDDLQALESELREQ---LEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERaRE 478
|
330
....*....|....*..
gi 1634229844 765 LMEAIQKQEEinfRLQD 781
Cdd:pfam12128 479 EQEAANAEVE---RLQS 492
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
583-774 |
4.42e-04 |
|
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: 43.96 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 583 SIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDR---LSHER------ 653
Cdd:pfam05557 282 SRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRvllLTKERdgyrai 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 654 ---------------HQFQRDKEAT------QELIEDLRKQLEHLQ----LLKLEAEQRRGRSSSMGLQEYH-----SRA 703
Cdd:pfam05557 362 lesydkeltmsnyspQLLERIEEAEdmtqkmQAHNEEMEAQLSVAEeelgGYKQQAQTLERELQALRQQESLadpsySKE 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1634229844 704 RESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKSLFSTA---FSESLAAEISSVSRDElMEAIQKQEE 774
Cdd:pfam05557 442 EVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKvlhLSMNPAAEAYQQRKNQ-LEKLQAEIE 514
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
516-728 |
4.63e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 516 RRVLELEKDTAATGEQHSRlRQENLQLVHRANALEEQLKEQELRACEMV---LEETRRQKELLCKMEREKSIEIENLQTR 592
Cdd:PTZ00121 1188 RKAEELRKAEDARKAEAAR-KAEEERKAEEARKAEDAKKAEAVKKAEEAkkdAEEAKKAEEERNNEEIRKFEEARMAHFA 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 593 LQQLDEENSELRsctpclKANIERLEEEKQKLLDEIESLTLRLSEEQENK---RRMGDRLSHERHQFQRDKEATQELIED 669
Cdd:PTZ00121 1267 RRQAAIKAEEAR------KADELKKAEEKKKADEAKKAEEKKKADEAKKKaeeAKKADEAKKKAEEAKKKADAAKKKAEE 1340
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1634229844 670 LRKqlehlqllKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDnrNLKEQNEE 728
Cdd:PTZ00121 1341 AKK--------AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD--AAKKKAEE 1389
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
29-209 |
4.72e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.01 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 29 AAQLAPGPAELRLGAPVGGPDPQSPGLDEPAPGAAADGGARwSAGPAPGLEGGPRDPGPSAPPPRSGPRgqlASPDAPGP 108
Cdd:PHA03307 56 VAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLA-PASPAREGSPTPPGPSSPDPPPPTPPP---ASPPPSPA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 109 GPRSEAPLPELDPLFSWTEEPEECG--PASCPESAPFRLQGSSSSHRARGEVDVFSPFPAPTAGELALEQGPGSPPQPSD 186
Cdd:PHA03307 132 PDLSEMLRPVGSPGPPPAASPPAAGasPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSS 211
|
170 180
....*....|....*....|...
gi 1634229844 187 LSQTHPLPSEPVGSQEDGPRLRA 209
Cdd:PHA03307 212 PISASASSPAPAPGRSAADDAGA 234
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
508-784 |
5.34e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.52 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 508 ADKVVFLERRVLELEK---DTAATGEQHSRLRQENLQLVHRANALEEQLKE-QELRAcemVLEETRRQKELLCKMEREKS 583
Cdd:pfam05622 127 SDKVKKLEATVETYKKkleDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKaNALRG---QLETYKRQVQELHGKLSEES 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 584 IEIENLQTRLQQLDEENselrsctpclkaniERLEEEKQKLLDEIESL-----TLRLSEEQENKRRMGDRLsHERHQFQR 658
Cdd:pfam05622 204 KKADKLEFEYKKLEEKL--------------EALQKEKERLIIERDTLretneELRCAQLQQAELSQADAL-LSPSSDPG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 659 DKEATQELIEDLRKQLEHLQL----LKLEAE-QRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGqi 733
Cdd:pfam05622 269 DNLAAEIMPAEIREKLIRLQHenkmLRLGQEgSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQK-- 346
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1634229844 734 iTLSIQGAKSLFSTAFSESLAAEIssvsrDELMEAiqkQEEINfRLQDYID 784
Cdd:pfam05622 347 -ALQEQGSKAEDSSLLKQKLEEHL-----EKLHEA---QSELQ-KKKEQIE 387
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
565-736 |
6.19e-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: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 565 LEETRRQK-ELLCKME---REKSIEIENLQTRLQQLDEENSELRSctpclkaNIERLEEEKQKLLDEIESLTLRLSEEQe 640
Cdd:pfam07888 36 LEECLQERaELLQAQEaanRQREKEKERYKRDREQWERQRRELES-------RVAELKEELRQSREKHEELEEKYKELS- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 641 nkrRMGDRLSHERHQFQRDKEATQ----ELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQ----EYHSRARESELEQ-- 710
Cdd:pfam07888 108 ---ASSEELSEEKDALLAQRAAHEarirELEEDIKTLTQRVLERETELERMKERAKKAGAQrkeeEAERKQLQAKLQQte 184
|
170 180
....*....|....*....|....*..
gi 1634229844 711 -EVRRLKQDNRNLKEQNEELNGQIITL 736
Cdd:pfam07888 185 eELRSLSKEFQELRNSLAQRDTQVLQL 211
|
|
| PRK14959 |
PRK14959 |
DNA polymerase III subunits gamma and tau; Provisional |
73-206 |
6.20e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 43.13 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 73 GPAPGLEGGPRDPGPSAPPPRSGPRGQLASPDAPGPGPRSEAPLPELdplfSWTEEPeecgpascpeSAPFRLQGssssh 152
Cdd:PRK14959 388 GPASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPAPSAAPSPRV----PWDDAP----------PAPPRSGI----- 448
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1634229844 153 rargevdvfSPFPAPTAGELALEQG-PGSPPQPSDLSQTHPLPSEPVGSQEDGPR 206
Cdd:PRK14959 449 ---------PPRPAPRMPEASPVPGaPDSVASASDAPPTLGDPSDTAEHTPSGPR 494
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
617-769 |
6.32e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 617 LEEEKQKLLDEIESLTLRLSEEQENKRR-MGDRLSHERHQFQRDKEATQEL---IEDLRKQLEHLQLlKLEAEQRRGRSS 692
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTeEEEEIRRLEEQVERLEAEVEELeaeLEEKDERIERLER-ELSEARSEERRE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 693 smglqeyHSRARE-SELEQEVRRLKQDNRNLKEQNEELNGQIITLsiqgaKSLFSTAFSESLAA--EISSVSRDELMEAI 769
Cdd:COG2433 461 -------IRKDREiSRLDREIERLERELEEERERIEELKRKLERL-----KELWKLEHSGELVPvkVVEKFTKEAIRRLE 528
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
33-186 |
7.16e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.24 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 33 APGPAELRLGAPVGGPDPQSPGLDEPAPGAAADGGARWSAGPAPGLEGGPRDPGPSAPPPRSGPrgqlasPDAPGPGPRS 112
Cdd:PHA03307 293 ERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRP------PPPADPSSPR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 113 EAPLPELDPLFSWTEEPEE--------CGPASCPESAPFRLQGSSSSHRARGEVDVFSPFPAPTA-GELALEQGPGSPPQ 183
Cdd:PHA03307 367 KRPRPSRAPSSPAASAGRPtrrraraaVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYPlLTPSGEPWPGSPPP 446
|
...
gi 1634229844 184 PSD 186
Cdd:PHA03307 447 PPG 449
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
75-217 |
7.40e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.24 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 75 APGLEGGPRDPGPSAPPPRSGPRGQLASPDAPG----------------------PGPRSEAPLPELDPLFSWTEEPEEC 132
Cdd:PHA03307 18 GEFFPRPPATPGDAADDLLSGSQGQLVSDSAELaavtvvagaaacdrfepptgppPGPGTEAPANESRSTPTWSLSTLAP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 133 GPAScPESAPFRLQGSSSSHRARGEVDVFSPFPAPTAGELALEQGPGSPPQPSDLSQTHPLPSEPVGSQEDGPRLRAVFD 212
Cdd:PHA03307 98 ASPA-REGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPL 176
|
....*
gi 1634229844 213 ALDGD 217
Cdd:PHA03307 177 SSPEE 181
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
517-801 |
7.42e-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: 43.11 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 517 RVLELEKDTAAtgEQHSRLRQENLQLVHRANALEEQLK-EQELRACEMVLEETRRQKELLCKMEREKSIEIE--NLQTRL 593
Cdd:TIGR00606 440 RTIELKKEILE--KKQEELKFVIKELQQLEGSSDRILElDQELRKAERELSKAEKNSLTETLKKEVKSLQNEkaDLDRKL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 594 QQLDEENSELRSCTPCLKaNIERLEEEKQKLLDEIESLTLRLSEEQ-------ENKRRMGDRLsherHQFQRDKEATQEL 666
Cdd:TIGR00606 518 RKLDQEMEQLNHHTTTRT-QMEMLTKDKMDKDEQIRKIKSRHSDELtsllgyfPNKKQLEDWL----HSKSKEINQTRDR 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 667 IEDLRKQLEhlqllKLEAEQRRGRSssmglQEYHSRARESELEQEV------RRLKQDNRNLKEQNEELNGQIITLSiqG 740
Cdd:TIGR00606 593 LAKLNKELA-----SLEQNKNHINN-----ELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLA--G 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 741 AKSLFSTAFSESLA----------------AEISSVSRD---ELMEAIQKQEEINFRLQDYIDR--IIVAIMETNPSILE 799
Cdd:TIGR00606 661 ATAVYSQFITQLTDenqsccpvcqrvfqteAELQEFISDlqsKLRLAPDKLKSTESELKKKEKRrdEMLGLAPGRQSIID 740
|
..
gi 1634229844 800 VK 801
Cdd:TIGR00606 741 LK 742
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
514-779 |
8.14e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 42.75 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 514 LERRVLELEKDTAATGEQHSRLRQENLQLVHRANALE--------------------EQLKEQELRAcemvleETRRQKE 573
Cdd:pfam05622 12 LAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLEsgddsgtpggkkylllqkqlEQLQEENFRL------ETARDDY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 574 LLCKMEREKsiEIENLQTR----------LQQLDEENSELRSCTPCLKANIERLEEEKQKLLDeIESL--TLRLSEEqEN 641
Cdd:pfam05622 86 RIKCEELEK--EVLELQHRneeltslaeeAQALKDEMDILRESSDKVKKLEATVETYKKKLED-LGDLrrQVKLLEE-RN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 642 KRRMGDRLSHERHqfQRDKEATQELIEDLRKQLEHLQlLKLEAEQRRGRSSSMGLQEYHsrARESELEQEVRRLKQDNRN 721
Cdd:pfam05622 162 AEYMQRTLQLEEE--LKKANALRGQLETYKRQVQELH-GKLSEESKKADKLEFEYKKLE--EKLEALQKEKERLIIERDT 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1634229844 722 LKEQNEEL---NGQIITLSIQGAKSLFSTAFSESLAAEISSVsrdELMEAIQKQEEINFRL 779
Cdd:pfam05622 237 LRETNEELrcaQLQQAELSQADALLSPSSDPGDNLAAEIMPA---EIREKLIRLQHENKML 294
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
504-731 |
8.36e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 504 EEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKS 583
Cdd:pfam10174 442 EEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKS 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 584 IEIEnlqtrLQQLDEENSELRSCTPclKA-NIERLEEEKQKLLDEIESLTLRLSEEQENKRRMG---DRLSHERHQFQRD 659
Cdd:pfam10174 522 LEIA-----VEQKKEECSKLENQLK--KAhNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQaevERLLGILREVENE 594
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1634229844 660 KEATQELIEDlrkqLEHLQLLKLEAEQRRGRSSSMGLQEyhSRARESELEQEVRRlKQDNRN---LKEQNEELNG 731
Cdd:pfam10174 595 KNDKDKKIAE----LESLTLRQMKEQNKKVANIKHGQQE--MKKKGAQLLEEARR-REDNLAdnsQQLQLEELMG 662
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
4-206 |
8.36e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.39 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 4 APPASPPGSEPPGPDPEPGGPDGPGAAQLAPGPAELRLGAPVGGPDPQSPGLDEPAPGAAADGGARwSAGPAPGLEGGPR 83
Cdd:PHA03247 2603 DDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRAR-RLGRAAQASSPPQ 2681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 84 DPGPSAPPPRSGPRGQLASPDAPGPGPRSeAPLPELDPLfswteePEECGPASCPESAPfrlqgsssshrargeVDVFSP 163
Cdd:PHA03247 2682 RPRRRAARPTVGSLTSLADPPPPPPTPEP-APHALVSAT------PLPPGPAAARQASP---------------ALPAAP 2739
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1634229844 164 FPAPTAGELALEQGPGSPPQPSdLSQTHPLPSEPVGSQEDGPR 206
Cdd:PHA03247 2740 APPAVPAGPATPGGPARPARPP-TTAGPPAPAPPAAPAAGPPR 2781
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
2-213 |
8.62e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.94 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 2 ASAPPASPPgseppgpDPEPGGPDGPGAAQLAPGPAELRLGAPVGGPDPQSPGLdEPAPGAAADGGARWSAGPAPGLEGG 81
Cdd:PRK12323 384 QPAPAAAAP-------AAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAP-EALAAARQASARGPGGAPAPAPAPA 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 82 PRdPGPSAPPPRSGPRGQ-LASPDAPGPGPRSEAPLPELDPLFSWTEEPEECGPASCPESAPFRLQGSSSSHRARGEVDV 160
Cdd:PRK12323 456 AA-PAAAARPAAAGPRPVaAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADP 534
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1634229844 161 FSPFPAPTAgelaleqGPGSPPQPSDLSQTHPLPSePVGSQEDGPRLRAVFDA 213
Cdd:PRK12323 535 DDAFETLAP-------APAAAPAPRAAAATEPVVA-PRPPRASASGLPDMFDG 579
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
535-742 |
1.05e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 535 LRQENLQLVHRANALEEQLK-EQEL--RACEM-VLEETRRQ--KELLCKMEReksiEIENLQTRLQQLDEENSELRSCTP 608
Cdd:pfam01576 31 LEKKHQQLCEEKNALQEQLQaETELcaEAEEMrARLAARKQelEEILHELES----RLEEEEERSQQLQNEKKKMQQHIQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 609 CLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDrlshERHQFQRDKEATQELIEDLRKQL-EHLQLLKLEAEQR 687
Cdd:pfam01576 107 DLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLED----QNSKLSKERKLLEERISEFTSNLaEEEEKAKSLSKLK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1634229844 688 RGRSSSMGLQEYHSRARES---ELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAK 742
Cdd:pfam01576 183 NKHEAMISDLEERLKKEEKgrqELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
552-733 |
1.10e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 552 QLK--EQELRACEMVLEETRRQK-ELLCKM-EREKSI-----EIENLQTRLQQLDEENSELrsctpclKANIERLEEEK- 621
Cdd:PRK11637 48 QLKsiQQDIAAKEKSVRQQQQQRaSLLAQLkKQEEAIsqasrKLRETQNTLNQLNKQIDEL-------NASIAKLEQQQa 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 622 --QKLL----------DEIESLTLRLSEEqENKRRmgdrlshERHQ--FQRDKEATQELIEDLRKQLEHLQLLKLEAEQR 687
Cdd:PRK11637 121 aqERLLaaqldaafrqGEHTGLQLILSGE-ESQRG-------ERILayFGYLNQARQETIAELKQTREELAAQKAELEEK 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1634229844 688 RGRSSS-MGLQ-------EYHSRARESELEQEVRRLKQDNRNLKE--QNE-ELNGQI 733
Cdd:PRK11637 193 QSQQKTlLYEQqaqqqklEQARNERKKTLTGLESSLQKDQQQLSElrANEsRLRDSI 249
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
585-785 |
1.14e-03 |
|
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: 42.75 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 585 EIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEK------QKLLDEIESL--TLRLSEEQENKRRMgDRLSHERHQF 656
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekaeryQALLKEKREYegYELLKEKEALERQK-EAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 657 QRDKEATQELIEDLRKQLEHL------------------------QLLKLEAEQRRGRSSsmgLQEYHSRAResELEQEV 712
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIeqlleelnkkikdlgeeeqlrvkeKIGELEAEIASLERS---IAEKERELE--DAEERL 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1634229844 713 RRLKQDNRNLKEQNEELNGQIITLSIQgakslfstafSESLAAEISSvSRDELMEAIQKQEEINFRLQDYIDR 785
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKR----------RDKLTEEYAE-LKEELEDLRAELEEVDKEFAETRDE 386
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1-205 |
1.18e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 1 MASAPPASPPGSEPPGPDPEPGGPDGPGAAQLAPGPAelrlgAPVGGPDPQ---------SPGLDEPAPGAAADGGARWS 71
Cdd:PHA03247 2737 AAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPA-----APAAGPPRRltrpavaslSESRESLPSPWDPADPPAAV 2811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 72 AGPAPGLEGGPRDPGPSAPPPRSGPrgqLASPDAPGPGPRSEAPLPELDPLFSWTEEPEECGPASCPeSAPFRLQGSSSS 151
Cdd:PHA03247 2812 LAPAAALPPAASPAGPLPPPTSAQP---TAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKP-AAPARPPVRRLA 2887
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1634229844 152 hrargevdvfSPFPAPTAGELALEQ-GPGSPPQPSDLSQTHPLPSEPVGSQEDGP 205
Cdd:PHA03247 2888 ----------RPAVSRSTESFALPPdQPERPPQPQAPPPPQPQPQPPPPPQPQPP 2932
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
615-785 |
1.26e-03 |
|
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: 42.42 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 615 ERLEEEKQKLLDEIESltLRLSEEQENKRRMG-DRLS-----HERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRR 688
Cdd:pfam17380 299 ERLRQEKEEKAREVER--RRKLEEAEKARQAEmDRQAaiyaeQERMAMERERELERIRQEERKRELERIRQEEIAMEISR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 689 GRS---SSMGLQEYHSRAREsELEQEVR-RLKQDNRNLKEQNEELNGQIITLSIQGAKSLFSTAFSESLAAEISSVSRDE 764
Cdd:pfam17380 377 MRElerLQMERQQKNERVRQ-ELEAARKvKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEE 455
|
170 180
....*....|....*....|....*.
gi 1634229844 765 L-----MEAIQKQEEINFRLQDYIDR 785
Cdd:pfam17380 456 QerqqqVERLRQQEEERKRKKLELEK 481
|
|
| BCAS2 |
pfam05700 |
Breast carcinoma amplified sequence 2 (BCAS2); This family consists of several eukaryotic ... |
531-636 |
1.28e-03 |
|
Breast carcinoma amplified sequence 2 (BCAS2); This family consists of several eukaryotic sequences of unknown function. The mammalian members of this family are annotated as breast carcinoma amplified sequence 2 (BCAS2) proteins. BCAS2 is a putative spliceosome associated protein.
Pssm-ID: 428593 [Multi-domain] Cd Length: 204 Bit Score: 41.03 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 531 QHSRLRQENLQLV--HRANA--LEEQLKEQELRACEMVLEETRRQKELLckmEREKSIEIENLQTRLQQLDEENSELRSc 606
Cdd:pfam05700 105 EHQRIRIENLELLqkYGANAwrLHNYQLEAILRRLEKELAETKEAIEEV---NRQRKNAQTAAGGELRSLEEKWKELVS- 180
|
90 100 110
....*....|....*....|....*....|
gi 1634229844 607 tpclkANIErLEEEKQKLLDEIESLTLRLS 636
Cdd:pfam05700 181 -----KNLE-IEAACEALEAEILELKRQAA 204
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
549-671 |
1.30e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.50 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 549 LEEQLKEQE-----LRACEMVLEETRRQKEllckMEREKSIEIENLQTRLQQLDEENSEL-----RSCTPCLKANIERLE 618
Cdd:pfam02841 178 LQEFLQSKEaveeaILQTDQALTAKEKAIE----AERAKAEAAEAEQELLREKQKEEEQMmeaqeRSYQEHVKQLIEKME 253
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1634229844 619 EEKQKLLDEIESLTLRLSEEQENKRRMGdrlsherhqFQRDKEATQELIEDLR 671
Cdd:pfam02841 254 AEREQLLAEQERMLEHKLQEQEELLKEG---------FKTEAESLQKEIQDLK 297
|
|
| Cluap1 |
pfam10234 |
Clusterin-associated protein-1; This protein is conserved from worms to humans. The protein of ... |
476-627 |
1.30e-03 |
|
Clusterin-associated protein-1; This protein is conserved from worms to humans. The protein of 413 amino acids contains a central coiled-coil domain, possibly the region that binds to clusterin. Cluap1 expression is highest in the nucleus and gradually increases during late S to G2/M phases of the cell cycle and returns to the basal level in the G0/G1 phases. In addition, it is upregulated in colon cancer tissues compared to corresponding non-cancerous mucosa. It thus plays a crucial role in the life of the cell.
Pssm-ID: 463013 [Multi-domain] Cd Length: 268 Bit Score: 41.41 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 476 KVARYLHQsgALTMEALEDPSPELMEGPEEDIADKVVFLeRRVLELEKDTAATG-------EQHSRLRQENLQLVHRANA 548
Cdd:pfam10234 86 KITSLLYN--AMKSADKEAEEEEDSTSSQFDLSSKLSDL-KAARQLASEITTKGaslydllGKEVDLREIRQQALSRPLE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 549 LEE---QLKEQeLRACEMVLEETRRQ--------KELLCKMEReKSIEIENLQTRLQQLdeenselRSCTPCLKANIERL 617
Cdd:pfam10234 163 IAEiekALKEA-IKNVAAEIEQTQKQlenlasdeANLEAKIEK-KKQELERNQKRLQTL-------QSVRPAFMDEYEKL 233
|
170
....*....|
gi 1634229844 618 EEEKQKLLDE 627
Cdd:pfam10234 234 EEELQKLYEE 243
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
540-637 |
1.60e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 41.25 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 540 LQLVHRANALEEQLKEqelraCEMVLEETRRQKELLCKmereksiEIENLQTRLQQLDEENSELRSctpclkaNIERLEE 619
Cdd:COG4026 124 LQNIPEYNELREELLE-----LKEKIDEIAKEKEKLTK-------ENEELESELEELREEYKKLRE-------ENSILEE 184
|
90
....*....|....*...
gi 1634229844 620 EKQKLLDEIESLTLRLSE 637
Cdd:COG4026 185 EFDNIKSEYSDLKSRFEE 202
|
|
| PHA03132 |
PHA03132 |
thymidine kinase; Provisional |
72-212 |
1.60e-03 |
|
thymidine kinase; Provisional
Pssm-ID: 222997 [Multi-domain] Cd Length: 580 Bit Score: 42.06 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 72 AGPAPGLEGGPRDPGPSAPPprSGPRGQLASPDAPGPGPRSEAPLPELDPlfswtEEPEECGPASCPEsapfrlqgSSSS 151
Cdd:PHA03132 56 PPRETGSGGGVATSTIYTVP--RPPRGPEQTLDKPDSLPASRELPPGPTP-----VPPGGFRGASSPR--------LGAD 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1634229844 152 HRARGevdvFSPFPAPTAGeLALEQGPGSPPQPSDLSQTH--PLPSEPVGSQEDGPRLRAVFD 212
Cdd:PHA03132 121 STSPR----FLYQVNFPVI-LAPIGESNSSSEELSEEEEHsrPPPSESLKVKNGGKVYPKGFS 178
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
554-725 |
1.75e-03 |
|
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: 41.86 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 554 KEQELRACEMVLEETRRQKELLCKMEREKSIEienlQTRLQQLDEENSELRSctpclkaniERLEEEKQKLLDEIESLTL 633
Cdd:pfam15709 328 REQEKASRDRLRAERAEMRRLEVERKRREQEE----QRRLQQEQLERAEKMR---------EELELEQQRRFEEIRLRKQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 634 RLSEEQ----ENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSR----ARE 705
Cdd:pfam15709 395 RLEEERqrqeEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRlmemAEE 474
|
170 180
....*....|....*....|....*...
gi 1634229844 706 SELE--------QEVRRLKQDNRNLKEQ 725
Cdd:pfam15709 475 ERLEyqrqkqeaEEKARLEAEERRQKEE 502
|
|
| bZIP_plant_BZIP46 |
cd14707 |
Basic leucine zipper (bZIP) domain of uncharaterized Plant BZIP transcription factors: a ... |
701-729 |
1.85e-03 |
|
Basic leucine zipper (bZIP) domain of uncharaterized Plant BZIP transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of uncharacterized plant bZIP transciption factors with similarity to Glycine max BZIP46, which may be a drought-responsive gene. Plant bZIPs are involved in developmental and physiological processes in response to stimuli/stresses such as light, hormones, and temperature changes. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.
Pssm-ID: 269855 [Multi-domain] Cd Length: 55 Bit Score: 36.91 E-value: 1.85e-03
10 20 30
....*....|....*....|....*....|...
gi 1634229844 701 SRAR----ESELEQEVRRLKQDNRNLKEQNEEL 729
Cdd:cd14707 16 SRARkqayTNELELEVAHLKEENARLKRQQEEL 48
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
44-197 |
2.18e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 41.59 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 44 PVGGPDPQSPGLDEPAPGAAAdggarWSAgpAPGLEGGPRDPGPSAPPPRSGPRGQLASPD-APGPGPRSEA-PLPELDP 121
Cdd:PHA03378 645 VLVFPTPHQPPQVEITPYKPT-----WTQ--IGHIPYQPSPTGANTMLPIQWAPGTMQPPPrAPTPMRPPAApPGRAQRP 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 122 LFSWTEEPEEC---GPASCPESAPFRL---QGSSSSHRARGEVDVFSPFPAPTAGELALEQGPGSPPQPSDLSQTHPLPS 195
Cdd:PHA03378 718 AAATGRARPPAaapGRARPPAAAPGRArppAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQ 797
|
..
gi 1634229844 196 EP 197
Cdd:PHA03378 798 PP 799
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
514-729 |
2.22e-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: 41.75 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 514 LERRVLELEKDTAATGEQHsrlrQENLQLVHraNALEEQLKEQELracemvleETRRQKELLCKMEREKSIEIENLQTRL 593
Cdd:pfam12128 327 LEDQHGAFLDADIETAAAD----QEQLPSWQ--SELENLEERLKA--------LTGKHQDVTAKYNRRRSKIKEQNNRDI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 594 QQLDEENSELRSCTPCLKANIER-LEEEKQKLLDEIESLTLRLSEEQEnkrRMGDRLSHERHQfQRDKEATQELIEDLRK 672
Cdd:pfam12128 393 AGIKDKLAKIREARDRQLAVAEDdLQALESELREQLEAGKLEFNEEEY---RLKSRLGELKLR-LNQATATPELLLQLEN 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1634229844 673 QLEHLQLLKLEAEQRRGRSSSMGLQEYHSRAREselEQEVRRLKQDNRNLKEQNEEL 729
Cdd:pfam12128 469 FDERIERAREEQEAANAEVERLQSELRQARKRR---DQASEALRQASRRLEERQSAL 522
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
2-209 |
2.33e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.70 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 2 ASAPPASPPGSEPPGPDPEPGGPDGPGAAQLAPGPAELRLGAPVGGPDPQSPGLDEPAPGAAADGGARWSagPAPGLEGG 81
Cdd:PHA03307 60 AACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPS--PAPDLSEM 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 82 PRDPGPSAPPPRSGPrgqLASPDAPGPGPRSEAPLPELDPLFSWTEEPEECgPASCPESAPFRLQGSSSSHRARGEVDVF 161
Cdd:PHA03307 138 LRPVGSPGPPPAASP---PAAGASPAAVASDAASSRQAALPLSSPEETARA-PSSPPAEPPPSTPPAAASPRPPRRSSPI 213
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1634229844 162 SPfPAPTAGELALEQGPGSPPQPSDLSQTHPLPSEPVGSQEDGPRLRA 209
Cdd:PHA03307 214 SA-SASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRP 260
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
610-729 |
2.46e-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: 39.89 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 610 LKANIERL---EEEKQKLLDEIesltlrlseEQENKrRMGDRLsherhqfqrdKEATQELIEdLRKQLEHLQLLKleaeq 686
Cdd:pfam13851 31 LKEEIAELkkkEERNEKLMSEI---------QQENK-RLTEPL----------QKAQEEVEE-LRKQLENYEKDK----- 84
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1634229844 687 rrgrsssMGLQEyhSRARESELEQEVRRLKQDNRNLKEQNEEL 729
Cdd:pfam13851 85 -------QSLKN--LKARLKVLEKELKDLKWEHEVLEQRFEKV 118
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
537-687 |
2.65e-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: 39.89 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 537 QENLQLVhraNALEEQ---LKEQElRACEMVLEET----RRQKELLCKMEREksieIENLQTRLQQLDEENSELRSctpc 609
Cdd:pfam13851 22 RNNLELI---KSLKEEiaeLKKKE-ERNEKLMSEIqqenKRLTEPLQKAQEE----VEELRKQLENYEKDKQSLKN---- 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1634229844 610 LKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEdlRKqlehLQLLKLEAEQR 687
Cdd:pfam13851 90 LKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLE--KK----LQALGETLEKK 161
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
585-764 |
2.76e-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: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 585 EIENLQTRLQQLDEENSELrsctpclKANIERLEEEKQKLLDEIESLTLRLSEEQEnkrRMGDRLsheRHQFQRDK---- 660
Cdd:COG3883 38 ELDALQAELEELNEEYNEL-------QAELEALQAEIDKLQAEIAEAEAEIEERRE---ELGERA---RALYRSGGsvsy 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 661 ------------------------EATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMgLQEYHSRARE-----SELEQE 711
Cdd:COG3883 105 ldvllgsesfsdfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEAL-KAELEAAKAEleaqqAEQEAL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1634229844 712 VRRLKQDNRNLKEQNEELNGQIITLSIQGAKSLFSTAFSESLAAEISSVSRDE 764
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
534-744 |
2.84e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 534 RLRQENLQLVHRANAL--EEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLK 611
Cdd:PLN02939 146 LLNQARLQALEDLEKIltEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 612 ANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGdRLSHERHQFQ---RDKEAT----QE--------LIEDLRKQLEH 676
Cdd:PLN02939 226 KELDVLKEENMLLKDDIQFLKAELIEVAETEERVF-KLEKERSLLDaslRELESKfivaQEdvsklsplQYDCWWEKVEN 304
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1634229844 677 LQLLkLEAEQRRGRSSSMGLQEYHsraresELEQEVRRLKQdnrNLKEQN-EELNGQIITLSIQGAKSL 744
Cdd:PLN02939 305 LQDL-LDRATNQVEKAALVLDQNQ------DLRDKVDKLEA---SLKEANvSKFSSYKVELLQQKLKLL 363
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
552-733 |
2.88e-03 |
|
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: 40.29 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 552 QLKEQELRACEMVLEEtrRQKELlckmeREKSIEIENLQTRLQQLDEENSELrsctpclKANIERLEEEKQKLLDEIESL 631
Cdd:COG1579 13 QELDSELDRLEHRLKE--LPAEL-----AELEDELAALEARLEAAKTELEDL-------EKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 632 TLRLSEEQENKRRmgDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRsssmglQEYHSRARESELEQE 711
Cdd:COG1579 79 EEQLGNVRNNKEY--EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAE------LEAELEEKKAELDEE 150
|
170 180
....*....|....*....|..
gi 1634229844 712 VRRLKQDNRNLKEQNEELNGQI 733
Cdd:COG1579 151 LAELEAELEELEAEREELAAKI 172
|
|
| EF-hand_6 |
pfam13405 |
EF-hand domain; |
206-235 |
2.88e-03 |
|
EF-hand domain;
Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 36.00 E-value: 2.88e-03
10 20 30
....*....|....*....|....*....|
gi 1634229844 206 RLRAVFDALDGDGDGFVRIEDFIQFATVYG 235
Cdd:pfam13405 1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
|
|
| bZIP |
cd14686 |
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ... |
702-733 |
3.69e-03 |
|
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.
Pssm-ID: 269834 [Multi-domain] Cd Length: 52 Bit Score: 35.98 E-value: 3.69e-03
10 20 30
....*....|....*....|....*....|..
gi 1634229844 702 RARESELEQEVRRLKQDNRNLKEQNEELNGQI 733
Cdd:cd14686 20 KERIEELEEEVEELEEENEELKAELEELRAEV 51
|
|
| Prefoldin_2 |
pfam01920 |
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
530-631 |
3.77e-03 |
|
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
Pssm-ID: 396482 [Multi-domain] Cd Length: 102 Bit Score: 37.59 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 530 EQHSRLRQENLQLVHRANALEEQLKEQE--LRACEMVLEETRRQK---ELLCKMEREKSieIENLQTRLQQLDEEnselr 604
Cdd:pfam01920 2 NKFQQLQQQLQLLAQQIKQLETQLKELElaLEELELLDEDTKVYKligDVLVKQDKEEV--KEQLEERKETLEKE----- 74
|
90 100
....*....|....*....|....*..
gi 1634229844 605 sctpclkanIERLEEEKQKLLDEIESL 631
Cdd:pfam01920 75 ---------IKTLEKQLEKLEKELEEL 92
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
580-645 |
3.77e-03 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 37.16 E-value: 3.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1634229844 580 REKSIEIENLQTRLQQLDEENSELrsctpclKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRM 645
Cdd:cd22887 7 QELEKRLAELEAELASLEEEIKDL-------EEELKEKNKANEILNDELIALQIENNLLEEKLRKL 65
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
20-185 |
3.80e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 20 EPGGPDGPGAAQLAPGPAELRLGAPVGGPDPQSPgldepapgaaadggarwSAGPAPGLEGGPRDPGpsAPPPRSGPRGQ 99
Cdd:PHA03247 2709 EPAPHALVSATPLPPGPAAARQASPALPAAPAPP-----------------AVPAGPATPGGPARPA--RPPTTAGPPAP 2769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 100 lASPDAPGPGPRSEAPLPELDPLFSWTEE-PEECGPASCPESAPFRLQGSSSSHRARGevdvfsPFPAPTAGELALEQGP 178
Cdd:PHA03247 2770 -APPAAPAAGPPRRLTRPAVASLSESRESlPSPWDPADPPAAVLAPAAALPPAASPAG------PLPPPTSAQPTAPPPP 2842
|
....*..
gi 1634229844 179 GSPPQPS 185
Cdd:PHA03247 2843 PGPPPPS 2849
|
|
| KLF14_N |
cd21576 |
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ... |
71-204 |
4.21e-03 |
|
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as Krueppel-like factor 14 or basic transcription element-binding protein 5/BTEB5) is a protein that in humans is encoded by the KLF14 gene. KLF14 regulates the transcription of various genes, including TGFbetaRII (the type II receptor for TGFbeta). KLF14 is expressed in many tissues, lacks introns, and is subject to parent-specific expression. It also appears to be a master regulator of gene expression in adipose tissue. KLF14 is associated with coronary artery disease, hypercholesterolemia, and type 2 diabetes. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF14 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF14.
Pssm-ID: 409238 [Multi-domain] Cd Length: 195 Bit Score: 39.42 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 71 SAGPAPGleggprDPGPSAPPPrsGPRGQLASPDAPGPGPRSEAPlPELDPLFSWTEEpeecGPASCPESAPfrLQGSSS 150
Cdd:cd21576 49 SALPGPG------PPGPAWVPP--LLQVPAPSPGAGGAAPHLLAA-SVLADLRGGAGE----GSREDSGEAP--RASSGS 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1634229844 151 SHRARGEVDVFSPFPAPTAGELALeQGPGSPPQPSDLSQTHPLPSEPVGSQEDG 204
Cdd:cd21576 114 SDPARGSSPTLGSEPAPASGEDAV-SGPESSFGAPAIPSAPAAPGAPAVSGEVP 166
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
515-675 |
4.24e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 39.72 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 515 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALeeQLKEQELRA-CEMVleetRRQKELL---CKMEREK-SIEIENL 589
Cdd:pfam17078 65 ERRLKDLEDQLSELKNSYEELTESNKQLKKRLENS--SASETTLEAeLERL----QIQYDALvdsQNEYKDHyQQEINTL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 590 QTRLQQLDEENSELrsctpcLKANIERLEEEK---QKLLDEIESLTLRLSEEQENK-RRMGDRLSHERHQFQRDK----- 660
Cdd:pfam17078 139 QESLEDLKLENEKQ------LENYQQRISSNDkdiDTKLDSYNNKFKNLDNIYVNKnNKLLTKLDSLAQLLDLPSwlnly 212
|
170
....*....|....*
gi 1634229844 661 EATQELIEDLRKQLE 675
Cdd:pfam17078 213 PESRNKILEYAEKME 227
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
580-794 |
4.29e-03 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 40.44 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 580 REKSIEIENLQTRLQQLDEENSELRSCTPCLKANieRLEEEKQKLLDEIESLTLRLSEEQENKRRMgDRLSHERHQFQ-- 657
Cdd:COG5244 82 KGGLVCESKGMDKDGEIKQENHEDRIHFEESKIR--RLEETIEALKSTEKEEIVELRRENEELDKI-NLSLRERISSEep 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 658 -RDKEATQ-------ELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEyhsrARESELEQEVRRLKQDNRNLKEQNEEL 729
Cdd:COG5244 159 eLNKDGSKlsydelkEFVEESRVQVYDMVELVSDISETLNRNGSIQRSS----VRECERSNIHDVLFLVNGILDGVIDEL 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1634229844 730 NGQIitlsiqgakslfstafsESLAAEISSvsrdeLMEAIQKQEEINFRLQDYIDRIIVAIMETN 794
Cdd:COG5244 235 NGEL-----------------ERLRRQLVS-----LMSSHGIEVEENSRLKATLEKFQSLELKVN 277
|
|
| ZapB |
pfam06005 |
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
615-676 |
4.80e-03 |
|
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.
Pssm-ID: 428718 [Multi-domain] Cd Length: 71 Bit Score: 36.48 E-value: 4.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1634229844 615 ERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDR---LSHERHQFQRDKEATQELIEDLRKQLEH 676
Cdd:pfam06005 7 EQLETKIQAAVDTIALLQMENEELKEENEELKEEaneLEEENQQLKQERNQWQERIRGLLGKLDE 71
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
483-675 |
4.91e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.33 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 483 QSGALTMEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTaatgEQHSR-LRQENLQLVHRANALEEQLKEQELRAC 561
Cdd:COG5185 380 DSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQI----EELQRqIEQATSSNEEVSKLLNELISELNKVMR 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 562 EMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIER-LEEEKQKLLDEIESLTLRLSEEQE 640
Cdd:COG5185 456 EADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERqLEGVRSKLDQVAESLKDFMRARGY 535
|
170 180 190
....*....|....*....|....*....|....*
gi 1634229844 641 NKRRmgdrlshERHQFQRDKEATQELIEDLRKQLE 675
Cdd:COG5185 536 AHIL-------ALENLIPASELIQASNAKTDGQAA 563
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
541-775 |
5.20e-03 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 39.99 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 541 QLVHRANALEEQLKEQELRACEMVLeetRRQKELLCKMEREKSIEIENLQTRLQQL------------DEENSELRSCTP 608
Cdd:pfam03999 71 RLLHEERDPFEPKKGMSLLQKEKKL---DTQLEHLRKEKAPRLAEIKELLEQLQQLceelgeeplpllIDPLPSLEELES 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 609 CLKaNIERLEEEKQKLLDEIESLtlrlseEQENKRRMGD-----RLSHERHQFQRDKEA---TQELIEDLRKQLEHLQLL 680
Cdd:pfam03999 148 FRK-HLENLRNEKERRLEEVNEL------KKQIKLLMEEldlvpGTDFEEDLLCESEDNfclSRENIDKLRKLIKQLEEQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 681 KLEAEQR----RGRSSSM--GLQ----EYHSRARESE---------LEQEVRRLKQDNR-NLKEQNEELNGQI-----IT 735
Cdd:pfam03999 221 KAEREEKiddlREKILELwnRLQvpqeEQESFVRENNslsqdtidaLREELQRLEELKKkNIKKLIEDLRVEIeelwdKL 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1634229844 736 LSIQGAKSLFSTAFSESLA--------AEISSV-----SRDELMEAIQKQEEI 775
Cdd:pfam03999 301 FYSTEQRKRFIPFFEELYTedllelheLELKRLkeeyeSNKEILELVEKWEEL 353
|
|
| MISS |
pfam15822 |
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ... |
32-198 |
5.56e-03 |
|
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.
Pssm-ID: 318115 [Multi-domain] Cd Length: 238 Bit Score: 39.20 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 32 LAPGPAELRLGAPVGGPDPQSPgldepapgaaadggarwsagpAPGLEGGPRDPGPSAPPPRSGPRGqlasPDAPGPGPR 111
Cdd:pfam15822 60 FGPAPTGMYPSIPLTGPSPGPP---------------------APFPPSGPSCPPPGGPYPAPTVPG----PGPIGPYPT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 112 SEAPLPELDPLFSWTEEPEECGPascpeSAPFrlqGSSSShrargevdvfSPFPAPTAGELALEQGPGSPPQPsdlsqtH 191
Cdd:pfam15822 115 PNMPFPELPRPYGAPTDPAAAAP-----SGPW---GSMSS----------GPWAPGMGGQYPAPNMPYPSPGP------Y 170
|
....*..
gi 1634229844 192 PLPSEPV 198
Cdd:pfam15822 171 PAVPPPQ 177
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
444-686 |
5.61e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 444 SQCHKQINRLE--DLSARLSDL-----EMNSPTKRLSSKK-VARYLHQSGALTMEALEDPSPELmEGPEEDIADkvvfLE 515
Cdd:PRK02224 190 DQLKAQIEEKEekDLHERLNGLeselaELDEEIERYEEQReQARETRDEADEVLEEHEERREEL-ETLEAEIED----LR 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 516 RRVLELEKDTAATGEQHSRLRQENLQLVHRANAL--EEQLKEQELRACEMVLEETRRQKELLCKMEREKSI-------EI 586
Cdd:PRK02224 265 ETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADAEAVEARREELEDRDEELRDRLEECRVaaqahneEA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 587 ENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTlrlSEEQENKRRMGD------RLSHERHQFQRDK 660
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE---EEIEELRERFGDapvdlgNAEDFLEELREER 421
|
250 260
....*....|....*....|....*.
gi 1634229844 661 EATQELIEDLRKQLEHLQLLKLEAEQ 686
Cdd:PRK02224 422 DELREREAELEATLRTARERVEEAEA 447
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
577-683 |
6.14e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.06 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 577 KMERE-KSIEIENLQTRLQQLDEENSEL-RSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERH 654
Cdd:COG0542 403 RMEIDsKPEELDELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
90 100
....*....|....*....|....*....
gi 1634229844 655 QFQRDKEATQELIEDLRKQLEHLQLLKLE 683
Cdd:COG0542 483 RYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
554-685 |
6.39e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 554 KEQELRACEmvlEETRRQKELLCKMEREksieIENLQTRLQQLDEENSELrscTPCLKANIE----------RLEEEKQK 623
Cdd:pfam01576 3 QEEEMQAKE---EELQKVKERQQKAESE----LKELEKKHQQLCEEKNAL---QEQLQAETElcaeaeemraRLAARKQE 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1634229844 624 LLDEIESLTLRLSEEQENKRrmgdrlsherhQFQRDKEATQELIEDLRKQLEH-------LQLLKLEAE 685
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQ-----------QLQNEKKKMQQHIQDLEEQLDEeeaarqkLQLEKVTTE 130
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
580-676 |
6.57e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 38.07 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 580 REKSIEI-ENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRL-SEEQENKRrmgdrlshERHQFQ 657
Cdd:pfam11559 47 RDRDLEFrESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLkTLEQKLKN--------EKEELQ 118
|
90
....*....|....*....
gi 1634229844 658 RdkeaTQELIEDLRKQLEH 676
Cdd:pfam11559 119 R----LKNALQQIKTQFAH 133
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
49-202 |
6.58e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.31 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 49 DPQSPGLDEPAPGAAADGGARWSAGPAPGLEGGPRDPGPSAPPPRSGPRGQLASPDAPGPGPRSEAPLPELDPlfswtee 128
Cdd:PHA03247 2700 DPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPP------- 2772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 129 peeCGPASCPESAPFRLQGSSSSHR------ARGEVDVFSPFPAPTAGELALEQ-GPGSPPQPSDLSQTHPLPSEPVGSQ 201
Cdd:PHA03247 2773 ---AAPAAGPPRRLTRPAVASLSESreslpsPWDPADPPAAVLAPAAALPPAASpAGPLPPPTSAQPTAPPPPPGPPPPS 2849
|
.
gi 1634229844 202 E 202
Cdd:PHA03247 2850 L 2850
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
555-778 |
7.95e-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: 39.95 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 555 EQELRACEMVLEETRRQkellCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLR 634
Cdd:TIGR00618 534 EQTYAQLETSEEDVYHQ----LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDM 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 635 LSEEQENKRRMGD------RLSHERHQFQRDKEA-----TQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRA 703
Cdd:TIGR00618 610 LACEQHALLRKLQpeqdlqDVRLHLQQCSQELALkltalHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEK 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 704 RE-----SELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKslfsTAFSESLAAEISSVSRDELMEAIQKQEEINFR 778
Cdd:TIGR00618 690 EQltywkEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD----LAAREDALNQSLKELMHQARTVLKARTEAHFN 765
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
552-729 |
8.04e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 552 QLKEQELRACEMVLEETRRQKELLC--KMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIE 629
Cdd:pfam01576 827 QSKESEKKLKNLEAELLQLQEDLAAseRARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTE 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 630 SLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELiEDLRKQLEhLQLLKLEAEQRRGRSSSMGLQEYHSRARESELE 709
Cdd:pfam01576 907 LLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQL-ERQNKELK-AKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLE 984
|
170 180
....*....|....*....|
gi 1634229844 710 QEVRRLKQDNRNLKEQNEEL 729
Cdd:pfam01576 985 QESRERQAANKLVRRTEKKL 1004
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
589-733 |
8.07e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 38.92 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 589 LQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERH------QFQRDKEA 662
Cdd:pfam15294 131 LHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGAKKDVKSNLKEISDLEEKmaalksDLEKTLNA 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1634229844 663 TQELIEDLRKQL---EHlQLLKleaeqrrgrsssmgLQEYHSRArESELEQEVRRLKQdNRNLKEQNEELNGQI 733
Cdd:pfam15294 211 STALQKSLEEDLastKH-ELLK--------------VQEQLEMA-EKELEKKFQQTAA-YRNMKEMLTKKNEQI 267
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
206-265 |
8.53e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 37.46 E-value: 8.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 206 RLRAVFDALDGDGDGFVRIEDFIQFAtvygAEQVKDLTKYLDPSGLGVISFEDFYQGITA 265
Cdd:COG5126 6 KLDRRFDLLDADGDGVLERDDFEALF----RRLWATLFSEADTDGDGRISREEFVAGMES 61
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
489-653 |
8.99e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 39.47 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 489 MEALEDPSPELMEGPEEDIADKVVFLERRVLELE------------------KDTAATGEQHSRLRQENLQLVHRANALE 550
Cdd:pfam02029 156 GEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKvkyeskvfldqkrghpevKSQNGEEEVTKLKVTTKRRQGGLSQSQE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 551 EQLKEQELRACEMVLEETRRQKEllcKMEREksiEIENLQTRLQQLDEENSELRsctpclKANIER---LEEEKQKLLDE 627
Cdd:pfam02029 236 REEEAEVFLEAEQKLEELRRRRQ---EKESE---EFEKLRQKQQEAELELEELK------KKREERrklLEEEEQRRKQE 303
|
170 180
....*....|....*....|....*.
gi 1634229844 628 IEsltLRLSEEQENKRRMGDRLSHER 653
Cdd:pfam02029 304 EA---ERKLREEEEKRRMKEEIERRR 326
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
534-662 |
9.63e-03 |
|
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: 38.53 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229844 534 RLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIeieNLQTRLQQLDEENSELRsctpclkan 613
Cdd:pfam13904 66 RQRQKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQQTKKREESH---KQKAAESASKSLAKPER--------- 133
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1634229844 614 iERLEEEKQKLLDEIESLTLRLSEEQENKRRMgDRLSHERHQFQRDKEA 662
Cdd:pfam13904 134 -KVSQEEAKEVLQEWERKKLEQQQRKREEEQR-EQLKKEEEEQERKQLA 180
|
|
| |
