|
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 ... |
716-756 |
6.27e-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: 71.99 E-value: 6.27e-16
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 7662234 716 SRDELMEAIQKQEEINFRLQDYIDRIIVAIMETNPSILEVK 756
Cdd:pfam09457 1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
470-742 |
8.43e-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: 78.56 E-value: 8.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 470 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQL---------KEQELRACEMVLEETRRQKELLCKMEREKSIE 540
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELeqlrkeleeLSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 541 IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDR---LSHERHQFQRDKEA 617
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 618 TQELIEDLRKQLEHL--QLLKLEAEQRRGRSS--------------SMGLQEYHSRARE--SELEQEVRRLKQDNRNLKE 679
Cdd:TIGR02168 836 TERRLEDLEEQIEELseDIESLAAEIEELEELieeleseleallneRASLEEALALLRSelEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7662234 680 QNEELNGQI--ITLSIQGAKSLFstafsESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRII 742
Cdd:TIGR02168 916 ELEELREKLaqLELRLEGLEVRI-----DNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
459-736 |
2.41e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 459 EEDIADKVVFLeRRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKEllckmEREKS 538
Cdd:COG1196 221 ELKELEAELLL-LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-----EYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 539 IEIENLQTRLQQLDEENSELRsctpclkANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEAT 618
Cdd:COG1196 295 AELARLEQDIARLEERRRELE-------ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 619 QELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKS 698
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270
....*....|....*....|....*....|....*...
gi 7662234 699 LFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQD 736
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
464-737 |
6.85e-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: 72.41 E-value: 6.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 464 DKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRAcEMVLEETRRQKEllckmereksiEIEN 543
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI-EQLEQEEEKLKE-----------RLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 544 LQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQ------------ENKRRMGDRLSH----- 606
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelskleEEVSRIEARLREieqkl 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 607 ------------ERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSsmgLQEYHSRARESELEQEVRRLKQDN 674
Cdd:TIGR02169 822 nrltlekeylekEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE---AALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 675 RNLKEQNEELNGQIITLSIQGA--KSLFSTAFS-----ESLAAEISSVS------------RDELMEAIQKQEEINFR-L 734
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSelKAKLEALEEelseiEDPKGEDEEIPeeelsledvqaeLQRVEEEIRALEPVNMLaI 978
|
...
gi 7662234 735 QDY 737
Cdd:TIGR02169 979 QEY 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
469-735 |
6.97e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 6.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 469 LERRVLELEKDtAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRL 548
Cdd:COG1196 198 LERQLEPLERQ-AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 549 QQLDEENSELRsctpclkANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQ 628
Cdd:COG1196 277 EELELELEEAQ-------AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 629 LEHLQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQgAKSLFSTAFSESL 708
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEE 428
|
250 260
....*....|....*....|....*..
gi 7662234 709 AAEISSVSRDELMEAIQKQEEINFRLQ 735
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELE 455
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
491-740 |
2.76e-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: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 491 RQENLQLVHRANA---LEEQLKEQE--LRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCL 565
Cdd:TIGR02168 666 AKTNSSILERRREieeLEEKIEELEekIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 566 KANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGR 645
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 646 SSSMglqeyhsRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKS-------LFSTAFSESLAAEISSvSRD 718
Cdd:TIGR02168 826 LESL-------ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELeselealLNERASLEEALALLRS-ELE 897
|
250 260
....*....|....*....|..
gi 7662234 719 ELMEAIQKQEEINFRLQDYIDR 740
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEE 919
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
500-694 |
2.86e-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: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 500 RANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKL 579
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 580 LDEIESLTLR---LSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQlLKLEAEQRRGRSSSMGLQEYHS 656
Cdd:TIGR02168 294 ANEISRLEQQkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK-EELESLEAELEELEAELEELES 372
|
170 180 190
....*....|....*....|....*....|....*...
gi 7662234 657 RAResELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQ 694
Cdd:TIGR02168 373 RLE--ELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
460-740 |
8.52e-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: 8.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 460 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELracEMVLEETRRQKELLCKMEREKSI 539
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA---EIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 540 E-----IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFqrd 614
Cdd:TIGR02168 785 EeleaqIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI--- 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 615 kEATQELIEDLRKQLEHL----------------QLLKLEAEQRRGRSSSMGLQEYHSRARES---------ELEQEVRR 669
Cdd:TIGR02168 862 -EELEELIEELESELEALlnerasleealallrsELEELSEELRELESKRSELRRELEELREKlaqlelrleGLEVRIDN 940
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7662234 670 LKQdnrNLKEQneelngQIITLSIQGAKSLFSTAFSESLAAEISSVSR--DEL----MEAIQKQEEINFRLqDYIDR 740
Cdd:TIGR02168 941 LQE---RLSEE------YSLTLEEAEALENKIEDDEEEARRRLKRLENkiKELgpvnLAAIEEYEELKERY-DFLTA 1007
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
463-729 |
1.92e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 463 ADKVVFLERRVLELEKDTAATGEQHSRLRQEnlqlvhrANALEEQLKEQELRACEMVLEETRRQKELL------CKMERE 536
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAE-------LQELEEKLEELRLEVSELEEEIEELQKELYalaneiSRLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 537 KSI---EIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEE----QENKRRMGD------R 603
Cdd:TIGR02168 304 KQIlreRLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELeaelEELESRLEEleeqleT 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 604 LSHERHQFQRDKEATQELIEDLRKQLEHlqllkLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEE 683
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLEARLER-----LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELER 458
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 7662234 684 LNGQIITLSIQGAKSlfSTAFSESLAAEISSVSRDELMEAIQKQEE 729
Cdd:TIGR02168 459 LEEALEELREELEEA--EQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
469-685 |
2.81e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 469 LERRV--LELEKDTAatgEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQT 546
Cdd:TIGR02168 198 LERQLksLERQAEKA---ERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 547 RLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLT---LRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIE 623
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLErqlEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7662234 624 DLRKQLEHLQLLKLEAEQR-----------RGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELN 685
Cdd:TIGR02168 355 SLEAELEELEAELEELESRleeleeqletlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
460-729 |
8.22e-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: 8.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 460 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANAL--EEQLKEQELRACEMVLEETRRQKELLCKMEREK 537
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 538 SIEIENLQTRL----QQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRrmgdrlshERHQFQR 613
Cdd:COG1196 322 EEELAELEEELeeleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE--------ELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 614 DKEATQELIEDLRKQLEHLQLLKLEAEQRRGRsssmgLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSI 693
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEE-----LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260 270
....*....|....*....|....*....|....*.
gi 7662234 694 QGAKSLFSTAFSESLAAEISSVSRDELMEAIQKQEE 729
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
459-697 |
1.32e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 459 EEDIADKVVFLERRVLELEKdtaaTGEQHSRLRQENLQLVHRANALEEQLKEQELRacemvLEETRRQKELLCKMEREkS 538
Cdd:PRK03918 216 LPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSKRKLEEKIRELEER-----IEELKKEIEELEEKVKE-L 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 539 IEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEK---QKLLDEIESLTLRLSEEQENKRRMGDRLS--HERHQFQR 613
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngiEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 614 DKEATQELIEDLRKQLEHLQLLKLEAEQrrgrsssmglqEYHSRAREsELEQEVRRLKQDNRNLKEQNEELNGQIITLsi 693
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKEL-----------EELEKAKE-EIEEEISKITARIGELKKEIKELKKAIEEL-- 431
|
....
gi 7662234 694 QGAK 697
Cdd:PRK03918 432 KKAK 435
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
460-747 |
1.72e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 460 EDIADKVVfleRRVLELEK-----DTAATGEQHSRLRQENLQ-LVHRANALEEQLKEQELRacemvLEETRRQKELLCKM 533
Cdd:PRK03918 144 DESREKVV---RQILGLDDyenayKNLGEVIKEIKRRIERLEkFIKRTENIEELIKEKEKE-----LEEVLREINEISSE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 534 EREKSIEIENLQTRLQQLD---EENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGD-------- 602
Cdd:PRK03918 216 LPELREELEKLEKEVKELEelkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeey 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 603 -RLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRsssmgLQEYhsRARESELEQEVRRLK------QDNR 675
Cdd:PRK03918 296 iKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER-----LEEL--KKKLKELEKRLEELEerhelyEEAK 368
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7662234 676 NLKEQNEELNGQIITLSIqgakslfstafsESLAAEISSVSR--DELMEAIQKQEEINFRLQDYIDRIIVAIME 747
Cdd:PRK03918 369 AKKEELERLKKRLTGLTP------------EKLEKELEELEKakEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
472-748 |
1.25e-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: 61.57 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 472 RVLELEKDTAAtgEQHSRLRQENLQ-------LVHRANALEEQLK---------EQELRACEMVLEETRRQKELLCKMER 535
Cdd:TIGR04523 415 KKLQQEKELLE--KEIERLKETIIKnnseikdLTNQDSVKELIIKnldntreslETQLKVLSRSINKIKQNLEQKQKELK 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 536 EKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRmgDRLSHERHQFQRDK 615
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK--ENLEKEIDEKNKEI 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 616 EATQELIEDLRKQLEHLQLL--KLEAEQRRGRSssmGLQEYHSRAreSELEQEVrrlkqdnRNLKEQNEELNGQIITlsI 693
Cdd:TIGR04523 571 EELKQTQKSLKKKQEEKQELidQKEKEKKDLIK---EIEEKEKKI--SSLEKEL-------EKAKKENEKLSSIIKN--I 636
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 7662234 694 QGAKslfstafsESLAAEISSVsRDELMEAIQKQEEINFRLQDYIDRI--IVAIMET 748
Cdd:TIGR04523 637 KSKK--------NKLKQEVKQI-KETIKEIRNKWPEIIKKIKESKTKIddIIELMKD 684
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
463-673 |
2.91e-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: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 463 ADKVVFLERRVLELEKDTAATGEQHSRLRQEnlqlvhrANALEEQlkeqeLRACEMVLEETRRQKELlckmeREKSIEIE 542
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAE-------LDALQER-----REALQRLAEYSWDEIDV-----ASAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 543 NLQTRLQQLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQR-DKEATQEL 621
Cdd:COG4913 672 ELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLEL 747
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 7662234 622 IEDLRKQLEHLQLLKLEAEQRRG-RSSSMGLQEYHSRAREsELEQEVRRLKQD 673
Cdd:COG4913 748 RALLEERFAAALGDAVERELRENlEERIDALRARLNRAEE-ELERAMRAFNRE 799
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
469-756 |
3.02e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.53 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 469 LERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLkeQELRAcemVLEETRRQKELLCKMEREKSIEIENLQTRL 548
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEEL--EQLRE---ELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 549 QQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIEsltlRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQ 628
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELE----ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 629 LEHLQllkleAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKSLFSTAFSESL 708
Cdd:COG4372 159 LESLQ-----EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 7662234 709 AAEISSVSRDELMEAIQKQEEINFRLQDYIDRIIVAIMETNPSILEVK 756
Cdd:COG4372 234 ALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIA 281
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
460-684 |
3.18e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 460 EDIADKVVFLERRVLELEKdtaaTGEQHSRLRQeNLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREksi 539
Cdd:PRK03918 469 KEIEEKERKLRKELRELEK----VLKKESELIK-LKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE--- 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 540 eIENLQTRLQQLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENK---------------------R 598
Cdd:PRK03918 541 -IKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELEELGFESVEELEERlkelepfyneylelkdaekelE 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 599 RMGDRLSHERHQFQRDKEATQEL---IEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARE--SELEQEVRRLKQD 673
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETekrLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAelEELEKRREEIKKT 695
|
250
....*....|.
gi 7662234 674 NRNLKEQNEEL 684
Cdd:PRK03918 696 LEKLKEELEER 706
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
453-688 |
1.69e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 453 ELMEGPEEDIAD------KVVFLERRVLELEKDTAATGEQHsRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQ 526
Cdd:PRK03918 321 EEINGIEERIKEleekeeRLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 527 KELLCKMEREKSIEIENLQTRLQQLDEENSELRS----CTPC---------------LKANIERLEEEKQKLLDEIESLT 587
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkCPVCgrelteehrkelleeYTAELKRIEKELKEIEEKERKLR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 588 LRLsEEQENKRRMGDRLSHERHQFQRDKEATQEL----IEDLRKQLEHLQLLKLEAEQRRGRSSSMGlqeyHSRARESEL 663
Cdd:PRK03918 480 KEL-RELEKVLKKESELIKLKELAEQLKELEEKLkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLK----KELEKLEEL 554
|
250 260
....*....|....*....|....*
gi 7662234 664 EQEVRRLKQDNRNLKEQNEELNGQI 688
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKEL 579
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
489-741 |
1.75e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 489 RLR--QENLQlvhRANALEEQLKEQelracemvLEETRRQKEllcKMER--EKSIEIENLQTRLQQLDEENselrsctpc 564
Cdd:COG1196 180 KLEatEENLE---RLEDILGELERQ--------LEPLERQAE---KAERyrELKEELKELEAELLLLKLRE--------- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 565 LKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQEL---IEDLRKQLEHLQLLKLEAEQ 641
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELlaeLARLEQDIARLEERRRELEE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 642 RRGRsssMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLsiQGAKSLFSTAFSESLAAEISsvSRDELM 721
Cdd:COG1196 317 RLEE---LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA--EEALLEAEAELAEAEEELEE--LAEELL 389
|
250 260
....*....|....*....|
gi 7662234 722 EAIQKQEEINFRLQDYIDRI 741
Cdd:COG1196 390 EALRAAAELAAQLEELEEAE 409
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
485-688 |
2.60e-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: 57.34 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 485 EQHSRLrQENLQLVHRANALEEQLKEQElracemvleetrrqkellcKMEREKSIEIENLQTRLQQLDEENSELRSCTPC 564
Cdd:TIGR04523 378 ENQSYK-QEIKNLESQINDLESKIQNQE-------------------KLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 565 LKANIERLEEEKQKLLDEIESLTlRLSEEQENKRrmgDRLSHERHQFQRDKEATQELIEDLRKqlehlQLLKLEAEQrrg 644
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLD-NTRESLETQL---KVLSRSINKIKQNLEQKQKELKSKEK-----ELKKLNEEK--- 505
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 7662234 645 rsssmglqeyhsrareSELEQEVRRLKQDNRNLKEQNEELNGQI 688
Cdd:TIGR04523 506 ----------------KELEEKVKDLTKKISSLKEKIEKLESEK 533
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
471-691 |
3.79e-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: 57.06 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 471 RRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEmvlEETRRQKELLCKMEREKSIEIEnlqtRLQQ 550
Cdd:pfam17380 395 RQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLE---EERAREMERVRLEEQERQQQVE----RLRQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 551 LDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLE 630
Cdd:pfam17380 468 QEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQE 547
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7662234 631 HlqllkleAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNlKEQNEELNGQIITL 691
Cdd:pfam17380 548 M-------EERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK-ARAEYEATTPITTI 600
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
460-731 |
3.89e-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: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 460 EDIADKvvflERRVLELEKDTAATGEQHSRLRQEnlqlvhrANALEEQLKEQELracemvlEETRRQKELlckmeREKSI 539
Cdd:TIGR04523 314 SELKNQ----EKKLEEIQNQISQNNKIISQLNEQ-------ISQLKKELTNSES-------ENSEKQREL-----EEKQN 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 540 EIE---------------------NLQTRLQQLDEENSELRSctpclkaNIERLEEEKQKLLDEIEsltlRLSEEQENKR 598
Cdd:TIGR04523 371 EIEklkkenqsykqeiknlesqinDLESKIQNQEKLNQQKDE-------QIKKLQQEKELLEKEIE----RLKETIIKNN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 599 RMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQL----LKLEAEQRRgrsssmglQEYHSRARE-SELEQEVRRLKQD 673
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRsinkIKQNLEQKQ--------KELKSKEKElKKLNEEKKELEEK 511
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7662234 674 NRNLKEQNEELNGQIITLSIQgaKSLFSTAFSeSLAAEISS----VSRDELMEAIQ-KQEEIN 731
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESE--KKEKESKIS-DLEDELNKddfeLKKENLEKEIDeKNKEIE 571
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
470-741 |
4.51e-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: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 470 ERRVLELEKDTAATGEQHSRLRQENLQLVhRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQ 549
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 550 QLDEENSELRSCTPCLKANIERL-EEEKQKLLDEIESLTLRLSE----EQENKRRMGDrLSHERHQFQRDKEATQELIED 624
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASlersIAEKERELED-AEERLAKLEAEIDKLLAEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 625 LRKQLEHLQLLK-----------------------LEAEQRRGRSSSMGLQEYHSRARE--SELEQEVRRLKQDNRNLKE 679
Cdd:TIGR02169 341 LEREIEEERKRRdklteeyaelkeeledlraeleeVDKEFAETRDELKDYREKLEKLKReiNELKRELDRLQEELQRLSE 420
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7662234 680 QNEELNGQIItlSIQGAKSLFSTAfSESLAAEISSvSRDELMEAIQKQEEIN---FRLQDYIDRI 741
Cdd:TIGR02169 421 ELADLNAAIA--GIEAKINELEEE-KEDKALEIKK-QEWKLEQLAADLSKYEqelYDLKEEYDRV 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
441-688 |
5.04e-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: 56.61 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 441 ALTMEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQ--ELRACEM 518
Cdd:TIGR02169 264 EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLlaEIEELER 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 519 VLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESL---TLRLSEEQE 595
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeeLQRLSEELA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 596 NKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQ--LLKLEAEQRRGRSSSMGLQ-EYHSRARE-SELEQEVRRLK 671
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAadLSKYEQELYDLKEEYDRVEkELSKLQRElAEAEAQARASE 503
|
250
....*....|....*..
gi 7662234 672 QDNRNLKEQNEELNGQI 688
Cdd:TIGR02169 504 ERVRGGRAVEEVLKASI 520
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
206-264 |
6.18e-08 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 49.94 E-value: 6.18e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7662234 206 RLRAVFDALDGDGDGFVRIEDFIQFATVYGA------EQVKDLTKYLDPSGLGVISFEDFYQGIT 264
Cdd:pfam13499 3 KLKEAFKLLDSDGDGYLDVEELKKLLRKLEEgeplsdEEVEELFKEFDLDKDGRISFEEFLELYS 67
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
201-264 |
9.78e-08 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 51.72 E-value: 9.78e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7662234 201 QEDGPRLRAVFDALDGDGDGFVRIEDFIQFATVYG--AEQVKDLTKYLDPSGLGVISFEDFYQGIT 264
Cdd:COG5126 65 ATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGvsEEEADELFARLDTDGDGKISFEEFVAAVR 130
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
480-698 |
1.01e-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: 54.77 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 480 TAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMV--LEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSE 557
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLkqLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 558 LRsctpclkANIERLEEEKQKLLDEI------ESLTLRLSEEQENK--------RRMGDRLSHERHQFQRDKEATQELIE 623
Cdd:COG4942 95 LR-------AELEAQKEELAELLRALyrlgrqPPLALLLSPEDFLDavrrlqylKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7662234 624 DLRKQLEHLQLLKLEAEQRRGRsssmgLQEYHSRARE--SELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKS 698
Cdd:COG4942 168 ELEAERAELEALLAELEEERAA-----LEALKAERQKllARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
500-688 |
1.18e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 500 RANALEEQLkeQELRACEMVLEETRRQKELLCKMeREKSIEIENLQTRLQQLDEENSELRS-----CTPCLKANIERLEE 574
Cdd:COG4913 226 AADALVEHF--DDLERAHEALEDAREQIELLEPI-RELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 575 EKQKLLDEIESLTLRLSEEQENKRRMgdRLSHERHQFQRdkeatqelIEDLRKQLEHLQLLKLEAEQRRGR--------- 645
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDEL--EAQIRGNGGDR--------LEQLEREIERLERELEERERRRARleallaalg 372
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 7662234 646 ----SSSMGLQEYHSRARE---------SELEQEVRRLKQDNRNLKEQNEELNGQI 688
Cdd:COG4913 373 lplpASAEEFAALRAEAAAllealeeelEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
454-686 |
1.23e-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: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 454 LMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKE--QELRACEMVLEETRRQKELLC 531
Cdd:pfam19220 31 QLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEElvARLAKLEAALREAEAAKEELR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 532 KMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLseeqenkrrmgDRLSHERHQF 611
Cdd:pfam19220 111 IELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERL-----------ALLEQENRRL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7662234 612 Q-RDKEATQELIEDLRKQLEHLQLlkLEAEQRRGR---SSSMGLQEYHSRArESELEQEVRRLKQDNRNLKEQNEELNG 686
Cdd:pfam19220 180 QaLSEEQAAELAELTRRLAELETQ--LDATRARLRaleGQLAAEQAERERA-EAQLEEAVEAHRAERASLRMKLEALTA 255
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
475-739 |
1.30e-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: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 475 ELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEE 554
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 555 NSELRSCTpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRmgdrlsHERHQFQRDKEATQELIEDLRKQLEHLQL 634
Cdd:pfam02463 261 EKEEEKLA--QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL------KLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 635 LKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQ-DNRNLKEQNEELNGQIITLSIQG-AKSLFSTAFSE-SLAAE 711
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQlEEELLAKKKLESERLSSAAKLKEeELELKSEEEKEaQLLLE 412
|
250 260
....*....|....*....|....*...
gi 7662234 712 ISSVSRDELMEAIQKQEEINFRLQDYID 739
Cdd:pfam02463 413 LARQLEDLLKEEKKEELEILEEEEESIE 440
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
488-694 |
2.62e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 488 SRLRQENLQLvHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSI---EIENLQTRLQQLDEENSELRsctpc 564
Cdd:COG4717 49 ERLEKEADEL-FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEEleeELEELEAELEELREELEKLE----- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 565 LKANIERLEEEKQKLLDEIESLTLRLsEEQENKRRmgdrlshERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRG 644
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERL-EELEERLE-------ELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 7662234 645 RSSSMGLQEyhSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQ 694
Cdd:COG4717 195 QDLAEELEE--LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
459-671 |
2.86e-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: 53.23 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 459 EEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQElracemvlEETRRQKELLCKMEREKS 538
Cdd:COG4942 50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK--------EELAELLRALYRLGRQPP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 539 IEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEkqklLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEAT 618
Cdd:COG4942 122 LALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAELEALLAELEEERAALEALKAER 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 7662234 619 QELIEDLRKQLEHL--QLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLK 671
Cdd:COG4942 198 QKLLARLEKELAELaaELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
464-741 |
3.08e-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: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 464 DKVVFLERRVLELEKDTAATGEQHSRLRQENLQLvhraNALEEQLKEQELRacemvLEETRRQKELLCKMEREKSIEIEN 543
Cdd:COG4913 654 AEYSWDEIDVASAEREIAELEAELERLDASSDDL----AALEEQLEELEAE-----LEELEEELDELKGEIGRLEKELEQ 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 544 LQTRLQQLDEENSELRSctPCLKANIERLEEEKQKLLDE------IESLTLRLSEEQENKRRMGDRLSHERHQFQRD-KE 616
Cdd:COG4913 725 AEEELDELQDRLEAAED--LARLELRALLEERFAAALGDaverelRENLEERIDALRARLNRAEEELERAMRAFNREwPA 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 617 ATQELIEDLRKQLEHLQLL-KLEAEqrrgrsssmGLQEYHSRARESELEQE-------VRRLKQDNRNLKEQNEELN--- 685
Cdd:COG4913 803 ETADLDADLESLPEYLALLdRLEED---------GLPEYEERFKELLNENSiefvadlLSKLRRAIREIKERIDPLNdsl 873
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7662234 686 -------GQIITLSIQGAKSLFSTAFSESLAAEISSVSRDElMEAIQKQEEinfRLQDYIDRI 741
Cdd:COG4913 874 kripfgpGRYLRLEARPRPDPEVREFRQELRAVTSGASLFD-EELSEARFA---ALKRLIERL 932
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
448-684 |
3.88e-07 |
|
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: 53.80 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 448 EDPSPELMEgpeedIADKVVFLERrvlELEKDTAATGEQHSRLRQ--ENLQLVHR----ANALEEQLKEQELRACEMVLE 521
Cdd:COG3096 832 PDPEAELAA-----LRQRRSELER---ELAQHRAQEQQLRQQLDQlkEQLQLLNKllpqANLLADETLADRLEELREELD 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 522 E-------TRRQKELLCKMEREKSI------EIENLQTRLQQLDEENSELRSCTPCLKANIERLE----EEKQKLLDE-- 582
Cdd:COG3096 904 AaqeaqafIQQHGKALAQLEPLVAVlqsdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGEns 983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 583 --IESLTLRLSEEQENKRRMGDRLSHERHQFQrdkEATQELI----------EDLRKQLEHLQLLKL----EAEQR-RGR 645
Cdd:COG3096 984 dlNEKLRARLEQAEEARREAREQLRQAQAQYS---QYNQVLAslkssrdakqQTLQELEQELEELGVqadaEAEERaRIR 1060
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 7662234 646 SSSMGLQEYHSRAR-----------ESELEQEVRRLKQDNRNLKEQNEEL 684
Cdd:COG3096 1061 RDELHEELSQNRSRrsqlekqltrcEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
446-696 |
5.69e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 446 ALEDPSPELMEgpeeDIADKVV--FLERRvLELEKDTAATgeqhsrlrqenlqlvhRANALEEQLKE--QELRACEMVLE 521
Cdd:COG3206 141 SYTSPDPELAA----AVANALAeaYLEQN-LELRREEARK----------------ALEFLEEQLPElrKELEEAEAALE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 522 ETRRQKELLCKMEREKSI--EIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLD--EIESLTLRLSEEQENK 597
Cdd:COG3206 200 EFRQKNGLVDLSEEAKLLlqQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAEL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 598 RRMGDRLShERHQfqrDKEATQELIEDLRKQLEH-----LQLLKLEAEQRRGRSSSMG--LQEYHSRARE-SELEQEVRR 669
Cdd:COG3206 280 AELSARYT-PNHP---DVIALRAQIAALRAQLQQeaqriLASLEAELEALQAREASLQaqLAQLEARLAElPELEAELRR 355
|
250 260
....*....|....*....|....*..
gi 7662234 670 LKQDNRNLKEQNEELNGQIITLSIQGA 696
Cdd:COG3206 356 LEREVEVARELYESLLQRLEEARLAEA 382
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
469-729 |
6.74e-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: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 469 LERRVLELEKdTAATGEQHSRLRQENLQLVHRANALEEQLKE----QELRACEMVLEETRRQKELLCKMEREKSIEIENl 544
Cdd:TIGR00618 417 SAFRDLQGQL-AHAKKQQELQQRYAELCAAAITCTAQCEKLEkihlQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA- 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 545 qtRLQQLDEENSELrsCTPCLKANIER----LEEEKQKLLDEIESLTLRLSEEQENKRRMGDRlshERHQFQRDKEATQE 620
Cdd:TIGR00618 495 --RLLELQEEPCPL--CGSCIHPNPARqdidNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTS---ERKQRASLKEQMQE 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 621 LIEDLRKQLEHLQLLKLEAEqrrgrsssmGLQEYHSRAR---ESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQgak 697
Cdd:TIGR00618 568 IQQSFSILTQCDNRSKEDIP---------NLQNITVRLQdltEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQ--- 635
|
250 260 270
....*....|....*....|....*....|..
gi 7662234 698 slfstAFSESLAAEISSVSRDELMEAIQKQEE 729
Cdd:TIGR00618 636 -----QCSQELALKLTALHALQLTLTQERVRE 662
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
470-643 |
7.72e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 470 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEEtrrqkellckmereksiEIENLQTRLQ 549
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA-----------------ELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 550 QLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENK-RRMGDRLSH---ERHQFQRDKEATQELIEDL 625
Cdd:COG4717 150 ELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEElqqRLAELEEELEEAQEELEEL 225
|
170
....*....|....*...
gi 7662234 626 RKQLEHLQLLKLEAEQRR 643
Cdd:COG4717 226 EEELEQLENELEAAALEE 243
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
470-682 |
8.76e-07 |
|
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: 8.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 470 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQElRACEMVLEETRRQK---ELLCKMEREKSieienlqT 546
Cdd:pfam05557 26 KRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAE-EALREQAELNRLKKkylEALNKKLNEKE-------S 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 547 RLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEdlr 626
Cdd:pfam05557 98 QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKE--- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 7662234 627 kqlehlqllkLEAEQRRGRSSSMGLQEYHSR-ARESELEQEVRRLKQDNRNLKEQNE 682
Cdd:pfam05557 175 ----------LEFEIQSQEQDSEIVKNSKSElARIPELEKELERLREHNKHLNENIE 221
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
469-696 |
8.93e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 8.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 469 LERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKE--QELRACEMVLEETRRQKELLCKMEREKSIEIEnLQT 546
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAElqEELEELEEELEELEAELEELREELEKLEKLLQ-LLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 547 RLQQLDEENSELRSCTPCLKANIERLEEEKQkLLDEIESLTLRLSEEQEnkrrmgdrlsHERHQFQRDKEATQELIEDLR 626
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRE-LEEELEELEAELAELQE----------ELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 627 KQLEHLQLLKLEAEQRRGRsssmglqeyhSRARESELEQEVRRLKQDNRNLKEQnEELNGQIITLSIQGA 696
Cdd:COG4717 199 EELEELQQRLAELEEELEE----------AQEELEELEEELEQLENELEAAALE-ERLKEARLLLLIAAA 257
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
444-738 |
1.09e-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: 52.33 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 444 MEALEDPSPELMEGPEEDIADKVVFLERrVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQL--KEQELRAcemvLE 521
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTE-IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlnIQKNIDK----IK 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 522 ETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELrsctpclKANIERLEEEKQKLLDEIES----LTLRLSEEQENK 597
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQL-------KDNIEKKQQEINEKTTEISNtqtqLNQLKDEQNKIK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 598 RRMGDRlsherhqfQRDKEATQELIEDLRKQLEHL--QLLKLEAEQRRGRSSSMG---------LQEYHSRARE-----S 661
Cdd:TIGR04523 267 KQLSEK--------QKELEQNNKKIKELEKQLNQLksEISDLNNQKEQDWNKELKselknqekkLEEIQNQISQnnkiiS 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 662 ELEQEVRRLKQ-------DNRNLKEQNEELNGQIITLSIQGAKSLFStafSESLAAEISsvsrdELMEAIQKQEEINFRL 734
Cdd:TIGR04523 339 QLNEQISQLKKeltnsesENSEKQRELEEKQNEIEKLKKENQSYKQE---IKNLESQIN-----DLESKIQNQEKLNQQK 410
|
....
gi 7662234 735 QDYI 738
Cdd:TIGR04523 411 DEQI 414
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
459-683 |
1.56e-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: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 459 EEDIADKVVFLERRvlelekdtAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMvLEETRRQKELLCKMEREks 538
Cdd:pfam13868 41 EERRLDEMMEEERE--------RALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEE-YEEKLQEREQMDEIVER-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 539 IEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESL--TLRLSEEQENKRRmgdrlsHERhqfQRDKE 616
Cdd:pfam13868 110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIleYLKEKAEREEERE------AER---EEIEE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7662234 617 ATQELIEDLRKQLEHLQLLKLEAEQRRGRsssMGLQEYHSRARESELEQEVRRLKQdNRNLKEQNEE 683
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDELRAK---LYQEEQERKERQKEREEAEKKARQ-RQELQQAREE 243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
460-677 |
1.61e-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: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 460 EDIADKVVFLERrVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSI 539
Cdd:COG4913 245 EDAREQIELLEP-IRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 540 EIENLQTRLQQLDEENselrsctpclkanIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQ 619
Cdd:COG4913 324 ELDELEAQIRGNGGDR-------------LEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 7662234 620 ELIEDLRKQLEHLQLLKLEAEQRRGRsssmglqeyhSRARESELEQEVRRLKQDNRNL 677
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRD----------LRRELRELEAEIASLERRKSNI 438
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
444-686 |
2.03e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 444 MEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEqlKEQELRACEMVLEET 523
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK--AKGKCPVCGRELTEE 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 524 RRqKELLckmeREKSIEIENLQTRLQQLDEENSELRSctPCLKANIERLEEEK----QKLLDEIESLTLRLS-------- 591
Cdd:PRK03918 449 HR-KELL----EEYTAELKRIEKELKEIEEKERKLRK--ELRELEKVLKKESEliklKELAEQLKELEEKLKkynleele 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 592 ---EEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMG-------------LQEYH 655
Cdd:PRK03918 522 kkaEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfesveeleerlkeLEPFY 601
|
250 260 270
....*....|....*....|....*....|....*.
gi 7662234 656 SR-----ARESELEQEVRRLKQDNRNLKEQNEELNG 686
Cdd:PRK03918 602 NEylelkDAEKELEREEKELKKLEEELDKAFEELAE 637
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
467-684 |
2.14e-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: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 467 VFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRA---------CEMVLE--ETRRQKELLCKMER 535
Cdd:pfam01576 127 VTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAkslsklknkHEAMISdlEERLKKEEKGRQEL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 536 EKSieIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDK 615
Cdd:pfam01576 207 EKA--KRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESER 284
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 616 EAtQELIEDLRKQL-EHLQLLKLEAEQRRGrsSSMGLQEYHSRaRESELEQEVRRLKQDNRNLKEQNEEL 684
Cdd:pfam01576 285 AA-RNKAEKQRRDLgEELEALKTELEDTLD--TTAAQQELRSK-REQEVTELKKALEEETRSHEAQLQEM 350
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
469-693 |
2.47e-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: 50.42 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 469 LERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLcKMEReksiEIENLQTRL 548
Cdd:pfam15558 85 REKQVIEKESRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQ-LQER----LEEACHKRQ 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 549 QQLDEENSELRSCTPCLKANIERL---------EEEKQKLLdeieSLTLRLSEEQEN-----KRR---MGDRLSHERHQF 611
Cdd:pfam15558 160 LKEREEQKKVQENNLSELLNHQARkvlvdcqakAEELLRRL----SLEQSLQRSQENyeqlvEERhreLREKAQKEEEQF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 612 QRDKEATQeliEDLRKQLEHLQLLKLEAEQRRGRS---SSMGLQEYHSRARESELEQEvrRLKQDNRNLKEQNEELNGQI 688
Cdd:pfam15558 236 QRAKWRAE---EKEEERQEHKEALAELADRKIQQArqvAHKTVQDKAQRARELNLERE--KNHHILKLKVEKEEKCHREG 310
|
....*
gi 7662234 689 ITLSI 693
Cdd:pfam15558 311 IKEAI 315
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
453-754 |
2.68e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 453 ELMEGPEEDIADKVvfleRRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCK 532
Cdd:PTZ00121 1538 EAKKAEEKKKADEL----KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 533 MEREKSIEIENLQtrlqqldeENSELRSCTPCLKanieRLEEEKQKLLDEIESltlrlsEEQENKRRMGDRLSHERHQFQ 612
Cdd:PTZ00121 1614 KAEEAKIKAEELK--------KAEEEKKKVEQLK----KKEAEEKKKAEELKK------AEEENKIKAAEEAKKAEEDKK 1675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 613 RDKEATQELiEDLRKQLEhlQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLS 692
Cdd:PTZ00121 1676 KAEEAKKAE-EDEKKAAE--ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7662234 693 IQGAKSLFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQdyIDRIIVAIMETNPSILE 754
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME--VDKKIKDIFDNFANIIE 1812
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
510-731 |
2.76e-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: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 510 EQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSEL-------------------RSCTPCLKANIE 570
Cdd:pfam05483 98 EAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLikennatrhlcnllketcaRSAEKTKKYEYE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 571 RlEEEKQKLLD---EIESLTLRLSE---EQENKR-RMGDRLSHERHQFQRDKEATQELIEDLRKQLEhLQLLKLEAEQRR 643
Cdd:pfam05483 178 R-EETRQVYMDlnnNIEKMILAFEElrvQAENARlEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVS-LLLIQITEKENK 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 644 GRSSSMGLQEyhSRARESELEQEVRRLKQDNRNLKEQNEELNGQI--ITLSIQGAKSLfSTAFSESLaaEISSVSRDELM 721
Cdd:pfam05483 256 MKDLTFLLEE--SRDKANQLEEKTKLQDENLKELIEKKDHLTKELedIKMSLQRSMST-QKALEEDL--QIATKTICQLT 330
|
250
....*....|.
gi 7662234 722 EAIQKQ-EEIN 731
Cdd:pfam05483 331 EEKEAQmEELN 341
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
460-633 |
3.47e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 460 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELlckmeREKSI 539
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI-----ERLEA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 540 EIENLQTRLQQLDEENSELRS--CTPCLKANIERLEEEKQKLLDEIESLTlRLSEEQENKRRMGDRLSHERHQFQRDKEA 617
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKklEEAELKELQAELEELEEELEELQEELE-RLEEALEELREELEEAEQALDAAERELAQ 486
|
170
....*....|....*.
gi 7662234 618 TQELIEDLRKQLEHLQ 633
Cdd:TIGR02168 487 LQARLDSLERLQENLE 502
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
462-694 |
3.49e-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: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 462 IADKVVFLERRVL-----ELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETrrQKELLCKMERE 536
Cdd:TIGR00618 585 DIPNLQNITVRLQdltekLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL--QLTLTQERVRE 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 537 KSI-----EIENLQTRLQQLDEENSELRSCTPCLkaniERLeEEKQKLLDEIESLTLRLSEEQEnkrrmgdRLSHERHQF 611
Cdd:TIGR00618 663 HALsirvlPKELLASRQLALQKMQSEKEQLTYWK----EML-AQCQTLLRELETHIEEYDREFN-------EIENASSSL 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 612 QRDKEATQELIEDLRKQLEHLQLLKL----EAEQRRGRSSSMGLQeyhsrareseLEQEVRRLKQDNRNLKEQNEELNGQ 687
Cdd:TIGR00618 731 GSDLAAREDALNQSLKELMHQARTVLkartEAHFNNNEEVTAALQ----------TGAELSHLAAEIQFFNRLREEDTHL 800
|
....*..
gi 7662234 688 IITLSIQ 694
Cdd:TIGR00618 801 LKTLEAE 807
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
464-672 |
3.55e-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: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 464 DKVVFLERRVLELEKDTAATGEQHSRLRQEnLQLVHRANALEEQLKE-----QELRACEMVLEETRRQKELLCKMER--- 535
Cdd:TIGR00618 219 ERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQlrariEELRAQEAVLEETQERINRARKAAPlaa 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 536 -EKSIE-----IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKL--LDEIESLTLRLSEEQENKRRMGDR---L 604
Cdd:TIGR00618 298 hIKAVTqieqqAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLqtLHSQEIHIRDAHEVATSIREISCQqhtL 377
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7662234 605 SHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRAREsELEQEVRRLKQ 672
Cdd:TIGR00618 378 TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ-ELQQRYAELCA 444
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
470-756 |
3.65e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 470 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKE-----QELRACEMVLEETRRQKELLCKMEREKSI-EIEN 543
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEElreleEELEELEAELAELQEELEELLEQLSLATEeELQD 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 544 LQTRLQQLDEENSELRsctpclkANIERLEEEKQKLLDEIESLTLRLSEEQENKRR------------------MGDRLS 605
Cdd:COG4717 197 LAEELEELQQRLAELE-------EELEEAQEELEELEEELEQLENELEAAALEERLkearlllliaaallallgLGGSLL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 606 HERHQ---------------FQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRL 670
Cdd:COG4717 270 SLILTiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 671 KQDNRNLKEQNEELNgqiITLSIQGAKSLFSTAFSESLAAEISSVSR-DELMEAIQKQEEINFRLQDYIDRIIVAIMETN 749
Cdd:COG4717 350 QELLREAEELEEELQ---LEELEQEIAALLAEAGVEDEEELRAALEQaEEYQELKEELEELEEQLEELLGELEELLEALD 426
|
....*..
gi 7662234 750 PSILEVK 756
Cdd:COG4717 427 EEELEEE 433
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
492-688 |
4.35e-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: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 492 QENLQLVHRANaleEQLKEQELRACEMVLEETRRQKELLCKMereksieienlqtRLQQLDEenselrsctpclkanIER 571
Cdd:pfam10168 531 QECLQLLSRAT---QVFREEYLKKHDLAREEIQKRVKLLKLQ-------------KEQQLQE---------------LQS 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 572 LEEEKQKLLDEIESLTLRLSEEQENK----RRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRgrsS 647
Cdd:pfam10168 580 LEEERKSLSERAEKLAEKYEEIKDKQeklmRRCKKVLQRLNSQLPVLSDAEREMKKELETINEQLKHLANAIKQAK---K 656
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 7662234 648 SMGLQEYHSRARESELEQEVRRLKQDNR-----NLKEQNEELNGQI 688
Cdd:pfam10168 657 KMNYQRYQIAKSQSIRKKSSLSLSEKQRktikeILKQLGSEIDELI 702
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
470-683 |
9.59e-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: 48.38 E-value: 9.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 470 ERRVLELEKDtaatgEQHSRLRQENLQLVHRANALEEQLKEQE----LRACEMVLEETRRQKELLCKMEREKSIEIENLQ 545
Cdd:pfam13868 87 QKRQEEYEEK-----LQEREQMDEIVERIQEEDQAEAEEKLEKqrqlREEIDEFNEEQAEWKELEKEEEREEDERILEYL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 546 TRLQQLDEEnselrsctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQF---QRDKEAT---- 618
Cdd:pfam13868 162 KEKAEREEE----------REAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERkerQKEREEAekka 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 619 ---QELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDN--RNLKEQNEE 683
Cdd:pfam13868 232 rqrQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEhrRELEKQIEE 301
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
470-582 |
9.97e-06 |
|
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: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 470 ERRVLELEKDTAATGEQHSR-LRQENLQLVHRANALEEQLKEQELR-ACEMVLEETRRQKELL------CKMEREKSIEI 541
Cdd:pfam14988 84 EREIQDLEEEKEKVRAETAEkDREAHLQFLKEKALLEKQLQELRILeLGERATRELKRKAQALklaakqALSEFCRSIKR 163
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 7662234 542 EN--LQTRLQQLDEEnselrscTPCLKANIERLEEEKQKLLDE 582
Cdd:pfam14988 164 ENrqLQKELLQLIQE-------TQALEAIKSKLENRKQRLKEE 199
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
493-636 |
1.35e-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: 47.70 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 493 ENLQLVHRANAL----EEQLKE--QELRACEMVLEETRRQ-KELLCKMEREKSIEIENLQTRLQQLDEENSELRSctpcl 565
Cdd:smart00787 151 ENLEGLKEDYKLlmkeLELLNSikPKLRDRKDALEEELRQlKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVK----- 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7662234 566 kaNIERLEEEKQKLLDEIESLTLRLSEEQenkrrmgDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLK 636
Cdd:smart00787 226 --KLEELEEELQELESKIEDLTNKKSELN-------TEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
426-642 |
1.53e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 48.41 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 426 RLSSKKVARYLHQSGALTMEALEDPSPELMEGPEEDIADKVVF----LERRVLELEKDTAATGEQHsRLRQENLQlvhRA 501
Cdd:pfam15709 296 RSSPTQTFVVTGNMESEEERSEEDPSKALLEKREQEKASRDRLraerAEMRRLEVERKRREQEEQR-RLQQEQLE---RA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 502 NALEEQLK-EQELRACEMVL------------EETRRQKELLCKMEREKS-IEIENLQTRLQQLDEENSElrsctpclkA 567
Cdd:pfam15709 372 EKMREELElEQQRRFEEIRLrkqrleeerqrqEEEERKQRLQLQAAQERArQQQEEFRRKLQELQRKKQQ---------E 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7662234 568 NIERLEEEKQKLldeiESLTLRLSEEQenKRRMG----DRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQR 642
Cdd:pfam15709 443 EAERAEAEKQRQ----KELEMQLAEEQ--KRLMEmaeeERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQ 515
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
485-673 |
1.55e-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: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 485 EQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLC--KMEREKSIEIENLQTRLQQLDEENSELRSCT 562
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESsrEIVKSYENELDPLKNRLKEIEHNLSKIMKLD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 563 PCLKAnIERLEEEKQKLLDEIESLTLR--------LSEEQENKRRMGDRLSHERHQFQRDkeatqelIEDLRKQLEHLQL 634
Cdd:TIGR00606 269 NEIKA-LKSRKKQMEKDNSELELKMEKvfqgtdeqLNDLYHNHQRTVREKERELVDCQRE-------LEKLNKERRLLNQ 340
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 7662234 635 LKLEAEQRRGRSS-SMGLQEYHSRARESELEQEVRRLKQD 673
Cdd:TIGR00606 341 EKTELLVEQGRLQlQADRHQEHIRARDSLIQSLATRLELD 380
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
460-755 |
1.69e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 460 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRacemvLEETRRQKELLCKMEREKSI 539
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE-----LAQAQEELESLQEEAEELQE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 540 EIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQ 619
Cdd:COG4372 116 ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 620 ELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARES---ELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGA 696
Cdd:COG4372 196 AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAlldALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 7662234 697 KSLFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRIIVAIMETNPSILEV 755
Cdd:COG4372 276 EELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
3-223 |
1.87e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 48.06 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 3 SAPPASPPGSEPPGPDPEPGGPDGPGAAQLAPGPAELRLGAPVGGPDPQSPGLDEPAPGAAADGGARWSAGPAPGLEGGP 82
Cdd:PRK07764 591 APGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWP 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 83 RDPGPSAPPPRSGPRGQLASPDAPGPGPRSEAPLPeldplfSWTEEPEecgPASCPESAPfRLQGSSSSHRARGEVDVFS 162
Cdd:PRK07764 671 AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAP------AATPPAG---QADDPAAQP-PQAAQGASAPSPAADDPVP 740
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7662234 163 PFPAPTAGELALEQGPGSPPQPSDLSQTHPLPSEPVGSQEDGPRLRAvfDALDGDGDGFVR 223
Cdd:PRK07764 741 LPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAE--DDAPSMDDEDRR 799
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
453-593 |
2.00e-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: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 453 ELMEGPEE--DIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKE----QELRACEMVLEETRRQ 526
Cdd:COG1579 25 RLKELPAElaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnKEYEALQKEIESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7662234 527 KELLCKMEREKSIEIENLQTRLQ----QLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEE 593
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAeleaELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
540-688 |
2.17e-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: 44.55 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 540 EIENLQTRLQQLDEEnselrsctpclkanIERLEEEKQKLLDEIESLTLRLSEEQENKRRmgdrlsherhQFQRDKEATQ 619
Cdd:pfam07926 2 ELSSLQSEIKRLKEE--------------AADAEAQLQKLQEDLEKQAEIAREAQQNYER----------ELVLHAEDIK 57
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7662234 620 ELiEDLRKQLEHLQL----LKLEAEQRRgrsSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQI 688
Cdd:pfam07926 58 AL-QALREELNELKAeiaeLKAEAESAK---AELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQL 126
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
569-748 |
2.39e-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: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 569 IERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSH----ERHQFQR-DKEATQELIEDLRKQLEHL-----QLLKLE 638
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlAEYSWDEiDVASAEREIAELEAELERLdassdDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 639 AEQRRgrsssmglqeyhSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLS------IQGAKSLFSTAFSESLAAEI 712
Cdd:COG4913 692 EQLEE------------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQdrleaaEDLARLELRALLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|....*.
gi 7662234 713 SSVSRDELMEAIQKQEEINFRLQDYIDRIIVAIMET 748
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
444-691 |
2.82e-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: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 444 MEALEDPSPELMEGPEEDIADKVvflERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQE-LRACEMV-LE 521
Cdd:pfam15921 247 LEALKSESQNKIELLLQQHQDRI---EQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNsMYMRQLSdLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 522 ETRRQ-KELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRM 600
Cdd:pfam15921 324 STVSQlRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 601 GDRlsherhqfqrdKEATQELIEDLRKQLE--HLQLLKLEAEQRRGRSSSMGLQEYHSRA---RESELEQE---VRRLKQ 672
Cdd:pfam15921 404 WDR-----------DTGNSITIDHLRRELDdrNMEVQRLEALLKAMKSECQGQMERQMAAiqgKNESLEKVsslTAQLES 472
|
250
....*....|....*....
gi 7662234 673 DNRNLKEQNEELNGQIITL 691
Cdd:pfam15921 473 TKEMLRKVVEELTAKKMTL 491
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
460-691 |
3.82e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 460 EDIADKVVFLERRVLELEKDTAATGEQHSRLrqenlqlvhranaleEQLKEQELRacemvLEETRRQKELLCKMEREKSI 539
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLERA---------------EDLVEAEDR-----IERLEERREDLEELIAERRE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 540 EIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLseeQENKRRMgDRLSHERHQFQRDKEATQ 619
Cdd:PRK02224 531 TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL---AELKERI-ESLERIRTLLAAIADAED 606
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7662234 620 ElIEDLRKQLEHLQLLKleaEQRRGRsssmgLQEyhSRARESELEQE-----VRRLKQDNRNLKEQNEELNGQIITL 691
Cdd:PRK02224 607 E-IERLREKREALAELN---DERRER-----LAE--KRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDEL 672
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
496-645 |
3.85e-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: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 496 QLVHRANALEEQLK--EQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEE-------------NSELRS 560
Cdd:COG1579 21 RLEHRLKELPAELAelEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyealQKEIES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 561 ctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHL------QL 634
Cdd:COG1579 101 ----LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELaakippEL 176
|
170
....*....|.
gi 7662234 635 LKLEAEQRRGR 645
Cdd:COG1579 177 LALYERIRKRK 187
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
471-735 |
3.87e-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: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 471 RRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLK-------------EQELRACEMVLEETRRQKELLCKMEREK 537
Cdd:pfam05557 72 REQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKnelselrrqiqraELELQSTNSELEELQERLDLLKAKASEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 538 SIEIENLQT----------RLQQLDEENSELRSCTPCLK------ANIERLEEEKQKLLDEIEsltlRLSEEQENKRRMG 601
Cdd:pfam05557 152 EQLRQNLEKqqsslaeaeqRIKELEFEIQSQEQDSEIVKnskselARIPELEKELERLREHNK----HLNENIENKLLLK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 602 DRLSHERHQFQRDKEATQELIeDLRKQLEHLQlLKLEAEQRRGRSSSMGLQeyhsraRESELEQEVRRLKQDNRNLKEQN 681
Cdd:pfam05557 228 EEVEDLKRKLEREEKYREEAA-TLELEKEKLE-QELQSWVKLAQDTGLNLR------SPEDLSRRIEQLQQREIVLKEEN 299
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 7662234 682 EELNGQIITLSIQGakslfstafsESLAAEISSVSRD--ELMEAIQKQEEINFRLQ 735
Cdd:pfam05557 300 SSLTSSARQLEKAR----------RELEQELAQYLKKieDLNKKLKRHKALVRRLQ 345
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
206-264 |
4.15e-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: 4.15e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7662234 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 ... |
469-673 |
5.82e-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: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 469 LERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRacemvLEETRRQK-ELLCKMEREKSiEIENLQTR 547
Cdd:pfam01576 375 LEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQAR-----LSESERQRaELAEKLSKLQS-ELESVSSL 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 548 LQQLDEENS----ELRSCTPCLKANIERLEEE-KQKLL---------DEIESLTLRLSEEQENKRRMGDRLSHERHQFQR 613
Cdd:pfam01576 449 LNEAEGKNIklskDVSSLESQLQDTQELLQEEtRQKLNlstrlrqleDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSD 528
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7662234 614 DKEATQELIEDLrKQLEhlqllklEAEQRRGRSSSMGLQEYHSRARESE-LEQEVRRLKQD 673
Cdd:pfam01576 529 MKKKLEEDAGTL-EALE-------EGKKRLQRELEALTQQLEEKAAAYDkLEKTKNRLQQE 581
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
497-672 |
6.90e-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: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 497 LVHRANALEEQLKEQELRACEmvLEETRRQKELLCK---MEREKSIEIENLQTRLQQLDEENSE-LRSCtpclkanIERL 572
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQ--QQNAERLLEEFCQrigQQLDAAEELEELLAELEAQLEELEEqAAEA-------VEQR 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 573 EEEKQKLlDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQrrgrsssmglq 652
Cdd:COG3096 581 SELRQQL-EQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDE----------- 648
|
170 180
....*....|....*....|
gi 7662234 653 eyhSRARESELEQEVRRLKQ 672
Cdd:COG3096 649 ---LAARKQALESQIERLSQ 665
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
489-682 |
7.26e-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: 46.27 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 489 RLRQENLQL-VHRANALEeQLKEQELRACEMV---LEETRRQKELlckmEREKSIEIENLQTRLQQLDEENSELRsctpc 564
Cdd:pfam17380 364 RIRQEEIAMeISRMRELE-RLQMERQQKNERVrqeLEAARKVKIL----EEERQRKIQQQKVEMEQIRAEQEEAR----- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 565 lKANIERLEEEKQKLLDEIESLTL-------RLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEdlrKQLEHLQLLKL 637
Cdd:pfam17380 434 -QREVRRLEEERAREMERVRLEEQerqqqveRLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE---KELEERKQAMI 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 7662234 638 EAEQRRgrssSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNE 682
Cdd:pfam17380 510 EEERKR----KLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE 550
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
471-680 |
8.30e-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: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 471 RRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMERE---KSIEIENLQTR 547
Cdd:pfam10174 232 QTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQElskKESELLALQTK 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 548 LQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQ--------------ENK-------RRMGDRLS- 605
Cdd:pfam10174 312 LETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKEsflnkktkqlqdltEEKstlageiRDLKDMLDv 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 606 HER--HQFQRDKEATQELIEDLRKQLEHLQ----------------LLKLE---AEQRRGRSSsmgLQEYHSRARESELE 664
Cdd:pfam10174 392 KERkiNVLQKKIENLQEQLRDKDKQLAGLKervkslqtdssntdtaLTTLEealSEKERIIER---LKEQREREDRERLE 468
|
250
....*....|....*.
gi 7662234 665 qEVRRLKQDNRNLKEQ 680
Cdd:pfam10174 469 -ELESLKKENKDLKEK 483
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
460-731 |
9.59e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 460 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEmvleETRRQKELLCKMEREKSI 539
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE----EKKKADELKKAEELKKAE 1561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 540 EIENLQTRLQQLDEENSELRsctpclKANIERLEEEKQklldeIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEAtq 619
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALR------KAEEAKKAEEAR-----IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-- 1628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 620 eliEDLRKQLEhlQLLKLEAEQRRgRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNgqiitlsiQGAKSL 699
Cdd:PTZ00121 1629 ---EEEKKKVE--QLKKKEAEEKK-KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK--------KAAEAL 1694
|
250 260 270
....*....|....*....|....*....|....
gi 7662234 700 FSTAFSESLAAEISSVSRDELMEA--IQKQEEIN 731
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAeeLKKAEEEN 1728
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
567-741 |
9.97e-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: 45.83 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 567 ANIERLEEEKQKLLDEIESLTLRLSEEQ---ENKRRMGDRLSHERHQFQRDKEATQELIEdlRKQLEHL-QLLKLEAEQR 642
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDliiDEKRQQLERLRREREKAERYQALLKEKRE--YEGYELLkEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 643 RGRSSSMGLQEyHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKSLfstafsESLAAEISSVsRDELME 722
Cdd:TIGR02169 241 AIERQLASLEE-ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKI------GELEAEIASL-ERSIAE 312
|
170
....*....|....*....
gi 7662234 723 AIQKQEEINFRLQDYIDRI 741
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEI 331
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
487-684 |
1.02e-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: 44.01 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 487 HSRLRQENLQLvhraNALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLqqldEENSELRSCTPcLK 566
Cdd:pfam14662 17 NQKLLQENSKL----KATVETREETNAKLLEENLNLRKQAKSQQQAVQKEKLLEEELEDLKL----IVNSLEEARRS-LL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 567 ANIERLEEEKQKLLDEIESLtlrlseEQENKRrmgdrLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRS 646
Cdd:pfam14662 88 AQNKQLEKENQSLLQEIESL------QEENKK-----NQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEK 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 7662234 647 SSMGLQEYHSRARESELEQEvrrLKQDNRNLKEQNEEL 684
Cdd:pfam14662 157 TTQIEELKSTVEEYSSIEEE---LRAEKSRLESQLPDM 191
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
500-694 |
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 7662234 500 RANALEEQLKEQELRAcEMVLEETRRQKEllcKMEREKSIEIEnlqtrlqqldEENSELRSctpclkanieRLEEEKQKL 579
Cdd:PRK12704 25 RKKIAEAKIKEAEEEA-KRILEEAKKEAE---AIKKEALLEAK----------EEIHKLRN----------EFEKELRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 580 LDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEyhsrAR 659
Cdd:PRK12704 81 RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEE----AK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 7662234 660 E---SELEQEVR-----RLKQDNRNLKEQNEELNGQIITLSIQ 694
Cdd:PRK12704 157 EillEKVEEEARheaavLIKEIEEEAKEEADKKAKEILAQAIQ 199
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
458-671 |
1.12e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 458 PEEDIADKVVFLERR-----VLELEKDTaatgEQHSRLRQENLQLVHRANALEEQLK-----EQELRACEMVLEET-RRQ 526
Cdd:PRK03918 497 KLKELAEQLKELEEKlkkynLEELEKKA----EEYEKLKEKLIKLKGEIKSLKKELEkleelKKKLAELEKKLDELeEEL 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 527 KELLCKMEREKSIEIENLQTRLQQLDE---ENSELRSCTPCLKANIERLEEEKQKLLD----------EIESLTLRLS-- 591
Cdd:PRK03918 573 AELLKELEELGFESVEELEERLKELEPfynEYLELKDAEKELEREEKELKKLEEELDKafeelaetekRLEELRKELEel 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 592 ------EEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGlqeyHSRARESELEQ 665
Cdd:PRK03918 653 ekkyseEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE----KALERVEELRE 728
|
....*.
gi 7662234 666 EVRRLK 671
Cdd:PRK03918 729 KVKKYK 734
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
460-688 |
1.12e-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: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 460 EDIADKVVFLErrvLELEKDTAATGEQHSRlrqeNLQLVHRANALEEQLKE-QELRAcemvlEETR---------RQKE- 528
Cdd:pfam01576 429 AELAEKLSKLQ---SELESVSSLLNEAEGK----NIKLSKDVSSLESQLQDtQELLQ-----EETRqklnlstrlRQLEd 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 529 ----LLCKMEREKSIEiENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMgdrl 604
Cdd:pfam01576 497 ernsLQEQLEEEEEAK-RNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL---- 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 605 sherhqfQRDKEATQELIEDLRKQLEHLQLL--KLEAEQRR-------GRSSSMGLQEYHSRARESELEQEVRRLK---- 671
Cdd:pfam01576 572 -------EKTKNRLQQELDDLLVDLDHQRQLvsNLEKKQKKfdqmlaeEKAISARYAEERDRAEAEAREKETRALSlara 644
|
250
....*....|....*...
gi 7662234 672 -QDNRNLKEQNEELNGQI 688
Cdd:pfam01576 645 lEEALEAKEELERTNKQL 662
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
449-687 |
1.35e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 449 DPSPELmegpeEDIADKVVFLERRVLELEkdtAATGEQHSRLRQ--ENLQLVHR----ANALEEQLKEQELRACEMVLEE 522
Cdd:PRK04863 834 DPEAEL-----RQLNRRRVELERALADHE---SQEQQQRSQLEQakEGLSALNRllprLNLLADETLADRVEEIREQLDE 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 523 T-------RRQKELLCKMEREKSI------EIENLQTRLQQLDEENSELRSCTPCLKANIERLE----EEKQKLLDEIES 585
Cdd:PRK04863 906 AeeakrfvQQHGNALAQLEPIVSVlqsdpeQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyEDAAEMLAKNSD 985
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 586 LTLRLSEEQENKRRMGDRLSHE----RHQFQRDKEATQELIEDLRKQLEHLQLLKLE-----------AEQR-RGRSSSM 649
Cdd:PRK04863 986 LNEKLRQRLEQAEQERTRAREQlrqaQAQLAQYNQVLASLKSSYDAKRQMLQELKQElqdlgvpadsgAEERaRARRDEL 1065
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 7662234 650 GLQEYHSRAR-----------ESELEQEVRRLKQDNRNLKEQNEELNGQ 687
Cdd:PRK04863 1066 HARLSANRSRrnqlekqltfcEAEMDNLTKKLRKLERDYHEMREQVVNA 1114
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
459-641 |
1.36e-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: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 459 EEDIADKVVFLERRVLELEKDtaatgeqHSRLRQENLQLVHRANALEEQLKEQELRACEmvLEEtrRQKELLCKME---- 534
Cdd:pfam04012 17 LDKAEDPEKMLEQAIRDMQSE-------LVKARQALAQTIARQKQLERRLEQQTEQAKK--LEE--KAQAALTKGNeela 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 535 REKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLE-------EEKQKLLDEIESLTLRlseEQENKRRMGDRLSHE 607
Cdd:pfam04012 86 REALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALEtkiqqlkAKKNLLKARLKAAKAQ---EAVQTSLGSLSTSSA 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 7662234 608 RHQFQR--DKEATQELIEDLRKQLEHLQLLKLEAEQ 641
Cdd:pfam04012 163 TDSFERieEKIEEREARADAAAELASAVDLDAKLEQ 198
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
535-742 |
1.44e-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: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 535 REKSIEIENLQTRLQQLDEENSELRSCTPCLKAN-IERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERhQFQR 613
Cdd:COG5185 242 ESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAEsSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEE-QLAA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 614 dKEATQELIEDLRKQLEHLQLLKLEAEQRRgRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSI 693
Cdd:COG5185 321 -AEAEQELEESKRETETGIQNLTAEIEQGQ-ESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQ 398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 7662234 694 QGAKSLFStaFSESLAAEISSVSRD--ELMEAIQKQEEINFRLQDYIDRII 742
Cdd:COG5185 399 NQRGYAQE--ILATLEDTLKAADRQieELQRQIEQATSSNEEVSKLLNELI 447
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
491-685 |
1.53e-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: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 491 RQENLQLVHRANALEEQLKE------QELRACEMVLEETRRQKELLCK--MEREKSIEIEN-----LQTR-------LQQ 550
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEmlrkvvEELTAKKMTLESSERTVSDLTAslQEKERAIEATNaeitkLRSRvdlklqeLQH 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 551 LDEENSELRSC-TPCLKANIERLEEEK--QKLLDEIESLTLRLSEEQenkrRMGDRLSHERHQFQRDkeatqelIEDLRK 627
Cdd:pfam15921 536 LKNEGDHLRNVqTECEALKLQMAEKDKviEILRQQIENMTQLVGQHG----RTAGAMQVEKAQLEKE-------INDRRL 604
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7662234 628 QLEHLQLLKLEAEQR----RGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNL----KEQNEELN 685
Cdd:pfam15921 605 ELQEFKILKDKKDAKirelEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLlnevKTSRNELN 670
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
491-692 |
1.64e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 491 RQENLQLVHRANALEEQLKE--QELRACEMVLEETRRQKEllckmerEKSIEIENLQTRLQQLDEENSELRSctpcLKAN 568
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAEldEEIERYEEQREQARETRD-------EADEVLEEHEERREELETLEAEIED----LRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 569 IERLEEEKQKLLDEIESLTLRLSE-EQENKRRMGD---------RLSHERHQFQRDKEATQELIEDLRKQLehlQLLKLE 638
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEElEEERDDLLAEaglddadaeAVEARREELEDRDEELRDRLEECRVAA---QAHNEE 343
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 7662234 639 AEQRRGRSSSmgLQEYHSRARE--SELEQEVRRLKQDNRNLKEQNEELNGQIITLS 692
Cdd:PRK02224 344 AESLREDADD--LEERAEELREeaAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
426-734 |
1.82e-04 |
|
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: 45.10 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 426 RLSSKKVARYLHQSGALTMEaLED------PSPELMEGPEED--IADKVVFlerrvlELEKDTAATGEQHSRLRQENLQL 497
Cdd:pfam05483 278 KLQDENLKELIEKKDHLTKE-LEDikmslqRSMSTQKALEEDlqIATKTIC------QLTEEKEAQMEELNKAKAAHSFV 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 498 VHRANA----LEEQLKEQELRacemvLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRsctpclkanieRLE 573
Cdd:pfam05483 351 VTEFEAttcsLEELLRTEQQR-----LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK-----------KIL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 574 EEKQKLLDEIESLTlRLSEEQENKRRMGDRLSHERHQFQRDKE------ATQE-----LIEDLRKQLEHLQLLKLEAEqr 642
Cdd:pfam05483 415 AEDEKLLDEKKQFE-KIAEELKGKEQELIFLLQAREKEIHDLEiqltaiKTSEehylkEVEDLKTELEKEKLKNIELT-- 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 643 rGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQgakslfstafSESLAAEISSVsRDELme 722
Cdd:pfam05483 492 -AHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK----------EMNLRDELESV-REEF-- 557
|
330
....*....|..
gi 7662234 723 aIQKQEEINFRL 734
Cdd:pfam05483 558 -IQKGDEVKCKL 568
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
469-680 |
1.97e-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: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 469 LERRVLELEKDTAATGEQHSRLRQEN------LQLVhrANALEEQLKEQElraCEmvlEETRRQKELLckmEREKSIEIE 542
Cdd:pfam04849 99 LTERNEALEEQLGSAREEILQLRHELskkddlLQIY--SNDAEESETESS---CS---TPLRRNESFS---SLHGCVQLD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 543 NLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKL-LDEIESLTL------RLSEEQENKRRmgdrlSHERHQfqrdK 615
Cdd:pfam04849 168 ALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLmSDCVEQLSEanqqmaELSEELARKME-----ENLRQQ----E 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7662234 616 EATQEL--IEDLRKQL-------EHLQLLkLEAEQRRGRSSSMGLQEYhsRARESELEQEVRRLKQDNRNLKEQ 680
Cdd:pfam04849 239 EITSLLaqIVDLQHKCkelgienEELQQH-LQASKEAQRQLTSELQEL--QDRYAECLGMLHEAQEELKELRKK 309
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
474-677 |
1.98e-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: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 474 LELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQldE 553
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG--E 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 554 ENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQ 633
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 7662234 634 LLKLEAEQR-RGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNL 677
Cdd:COG1196 735 EELLEELLEeEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
76-205 |
2.01e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.87 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 76 PGLEGGPRDPGPSAPPPRSGPRGQLASPDAPGPGPRSEAPLPELDPLFSWTEEPEECGPASCPESAPFRLQGSSSSHRAR 155
Cdd:PRK12323 365 PGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGP 444
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 7662234 156 GEVD--VFSPFPAPTAGELALEQGPGSPPQPSDLSQTHPLPSEPVGSQEDGP 205
Cdd:PRK12323 445 GGAPapAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDP 496
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
517-643 |
2.07e-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: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 517 EMVLEETRRqkELLCKMEREKSIEIENLQTRLQQLDEENSELRSctpclkaNIERLEEEKQKLLDEIESLTLRLSEEQEN 596
Cdd:COG2433 379 EEALEELIE--KELPEEEPEAEREKEHEERELTEEEEEIRRLEE-------QVERLEAEVEELEAELEEKDERIERLERE 449
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 7662234 597 KRRMGDRlshERHQFQRDKEAT--QELIEDLRKQLEHLQ--LLKLEAEQRR 643
Cdd:COG2433 450 LSEARSE---ERREIRKDREISrlDREIERLERELEEERerIEELKRKLER 497
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
504-688 |
2.19e-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: 44.84 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 504 LEEQLK--EQELRACEMVLEETRRQKELLCKMEReksieieNLQTRLQQLDEENSELRSctpclkaNIERLEEEKQKLLD 581
Cdd:pfam09726 400 LEQDIKklKAELQASRQTEQELRSQISSLTSLER-------SLKSELGQLRQENDLLQT-------KLHNAVSAKQKDKQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 582 EIESLTLRLSEEQENKRRMGDRLSHERhQFQRDKEATQEliedlrkqlehlQLLKLEAEQRRGRSSSMglqeyhsRARES 661
Cdd:pfam09726 466 TVQQLEKRLKAEQEARASAEKQLAEEK-KRKKEEEATAA------------RAVALAAASRGECTESL-------KQRKR 525
|
170 180
....*....|....*....|....*..
gi 7662234 662 ELEQEVRRLKQDNRNLKEQNEELNGQI 688
Cdd:pfam09726 526 ELESEIKKLTHDIKLKEEQIRELEIKV 552
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
517-741 |
2.47e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 517 EMVLEETRRQKELLcKMEREKSIE-----IENLQTRLQQLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLS 591
Cdd:COG1340 7 SSSLEELEEKIEEL-REEIEELKEkrdelNEELKELAEKRDELNAQVKE----LREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 592 EEQENKRRMGDRLshERHQFQRDKEATQEL-IEDLRKQLEHL------QLLKLEAEQRR-GRSSSMGlQEYHSRARESEL 663
Cdd:COG1340 82 ELNEKLNELREEL--DELRKELAELNKAGGsIDKLRKEIERLewrqqtEVLSPEEEKELvEKIKELE-KELEKAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 664 EQEVRRLKQDNRNLKEQNEELNGQIITLS--IQGAKSLFSTAFSEslaaeissvsRDELM-EAIQKQEEINfRLQDYIDR 740
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKELAeeAQELHEEMIELYKE----------ADELRkEADELHKEIV-EAQEKADE 227
|
.
gi 7662234 741 I 741
Cdd:COG1340 228 L 228
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
82-243 |
2.71e-04 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 43.70 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 82 PRDPGPSAPPPRsgPRGQLASPDAPGPGPRSEAPLPELDPLFSWTEEPeecgPASCPESAPFRLQGSSSSHRARGEVDVF 161
Cdd:PHA02682 81 PLAPSPACAAPA--PACPACAPAAPAPAVTCPAPAPACPPATAPTCPP----PAVCPAPARPAPACPPSTRQCPPAPPLP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 162 SPFPAPTAGELALEQGPGSPPQPSDLSQThpLPSEPVGSQEDGPRLRAvfDALDGDGDGfvriEDFIQFATVYGAEQVKD 241
Cdd:PHA02682 155 TPKPAPAAKPIFLHNQLPPPDYPAASCPT--IETAPAASPVLEPRIPD--KIIDADNDD----KDLIKKELADIADSVRD 226
|
..
gi 7662234 242 LT 243
Cdd:PHA02682 227 LN 228
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
445-685 |
2.94e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 445 EALEDPspELMEGPE---------EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQE--- 512
Cdd:TIGR02169 779 EALNDL--EARLSHSripeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEkei 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 513 ------LRACEMVLEETRRQKELLCKMEREKSIEIENLQtrlqqldeenselrsctpclkANIERLEEEKQKLLDEIESL 586
Cdd:TIGR02169 857 enlngkKEELEEELEELEAALRDLESRLGDLKKERDELE---------------------AQLRELERKIEELEAQIEKK 915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 587 TLRLSEEQENKRRMGDRLSHERHQFQRDKEATQEL--IEDLRKQLEhlqllKLEAEQRRGRSSSMG-LQEYH-SRARESE 662
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElsLEDVQAELQ-----RVEEEIRALEPVNMLaIQEYEeVLKRLDE 990
|
250 260
....*....|....*....|...
gi 7662234 663 LEQEVRRLKQDNRNLKEQNEELN 685
Cdd:TIGR02169 991 LKEKRAKLEEERKAILERIEEYE 1013
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
544-691 |
3.07e-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: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 544 LQTRLQQLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEA-----T 618
Cdd:COG1579 12 LQELDSELDRLEHRLKE----LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7662234 619 QELIEDLRKQLEHLQLLKLEAEQRRgrsssMGLQEYHSRAR------ESELEQEVRRLKQDNRNLKEQNEELNGQIITL 691
Cdd:COG1579 88 NKEYEALQKEIESLKRRISDLEDEI-----LELMERIEELEeelaelEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
460-728 |
3.08e-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: 44.27 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 460 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRqkellCKMEREKSI 539
Cdd:TIGR00606 785 KVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK-----LIQDQQEQI 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 540 EI----------------ENLQTRLQ---QLDEENSELRSCTPCLKANIER---LEEEKQKLLDEIESLTLRLSEE---- 593
Cdd:TIGR00606 860 QHlksktnelkseklqigTNLQRRQQfeeQLVELSTEVQSLIREIKDAKEQdspLETFLEKDQQEKEELISSKETSnkka 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 594 ----QENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGR-SSSMGLQEYH---SRARESELEQ 665
Cdd:TIGR00606 940 qdkvNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKiNEDMRLMRQDidtQKIQERWLQD 1019
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7662234 666 EVRRLKQDNRnLKEQNEEL---NGQIITLSIQGAKSLFstafsESLAAEISSVSRDELMEAIQKQE 728
Cdd:TIGR00606 1020 NLTLRKRENE-LKEVEEELkqhLKEMGQMQVLQMKQEH-----QKLEENIDLIKRNHVLALGRQKG 1079
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
466-631 |
3.24e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 466 VVFLERRVLELEkdtaatgEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKEllckmerEKSIEIENLQ 545
Cdd:PRK12705 22 VVLLKKRQRLAK-------EAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE-------ELQREEERLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 546 TRLQQLDEENselrsctpclkaniERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLshERHQFQRDKEATQELIEDL 625
Cdd:PRK12705 88 QKEEQLDARA--------------EKLDNLENQLEEREKALSARELELEELEKQLDNEL--YRVAGLTPEQARKLLLKLL 151
|
....*.
gi 7662234 626 RKQLEH 631
Cdd:PRK12705 152 DAELEE 157
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
444-744 |
3.45e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 444 MEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQE--NLQLVHRANALEEQLKEQE--------- 512
Cdd:COG4717 179 LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEleQLENELEAAALEERLKEARlllliaaal 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 513 ----------------------LRACEMVLEETRRQKEllcKMEREKSIEIENLQTRLQQLDEEnsELRSCTPCLKANIE 570
Cdd:COG4717 259 lallglggsllsliltiagvlfLVLGLLALLFLLLARE---KASLGKEAEELQALPALEELEEE--ELEELLAALGLPPD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 571 RLEEEKQKLLDEIESLTLRLSEEQENKRRMgDRLSHERHQFQRDKEATQELIEDLRKQLEHLQ-LLKLEAE----QRRGR 645
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEELRAALEQAEeYQELKEEleelEEQLE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 646 SSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSiqgakslfstafseslaAEISSVSRD-ELMEAI 724
Cdd:COG4717 413 ELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELE-----------------AELEQLEEDgELAELL 475
|
330 340
....*....|....*....|
gi 7662234 725 QKQEEINFRLQDYIDRIIVA 744
Cdd:COG4717 476 QELEELKAELRELAEEWAAL 495
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
464-688 |
3.74e-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: 43.73 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 464 DKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRAC--EMVLEETRRQKELLCKMEREKSIEI 541
Cdd:pfam07888 94 EKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLerETELERMKERAKKAGAQRKEEEAER 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 542 ENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQ----ENKRRMGD-RLSHER-HQFQRDK 615
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHrkeaENEALLEElRSLQERlNASERKV 253
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7662234 616 EATQELIEDLRKQLEH----LQLLKLEAEQRRGRSSSMGLQEYHSRARESeleQEVRRLKQDNRNLKEQNEELNGQI 688
Cdd:pfam07888 254 EGLGEELSSMAAQRDRtqaeLHQARLQAAQLTLQLADASLALREGRARWA---QERETLQQSAEADKDRIEKLSAEL 327
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
453-747 |
3.87e-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: 44.27 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 453 ELMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEE------QLKEQELRACEMVLEETRRQ 526
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSlireikDAKEQDSPLETFLEKDQQEK 925
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 527 KELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQkllDEIESLTLRLSEEQENKRRMGDRLSH 606
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKE---TELNTVNAQLEECEKHQEKINEDMRL 1002
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 607 ERHQFQRDKEATQELIEDL--RKQLEHLQLLKLEAEQRRGRSSSMGLQEyhSRARESELEQEVRRLKQDNRNLKEQNEEL 684
Cdd:TIGR00606 1003 MRQDIDTQKIQERWLQDNLtlRKRENELKEVEEELKQHLKEMGQMQVLQ--MKQEHQKLEENIDLIKRNHVLALGRQKGY 1080
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7662234 685 NGQIItlsiqgaksLFSTAFSESLAAEISSVSRDELMEaIQKQEEINFRLQDYIDRIIVAIME 747
Cdd:TIGR00606 1081 EKEIK---------HFKKELREPQFRDAEEKYREMMIV-MRTTELVNKDLDIYYKTLDQAIMK 1133
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
538-729 |
3.90e-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: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 538 SIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDR---LSHER------ 608
Cdd:pfam05557 282 SRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRvllLTKERdgyrai 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 609 ---------------HQFQRDKEAT------QELIEDLRKQLEHLQ----LLKLEAEQRRGRSSSMGLQEYH-----SRA 658
Cdd:pfam05557 362 lesydkeltmsnyspQLLERIEEAEdmtqkmQAHNEEMEAQLSVAEeelgGYKQQAQTLERELQALRQQESLadpsySKE 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7662234 659 RESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKSLFSTA---FSESLAAEISSVSRDElMEAIQKQEE 729
Cdd:pfam05557 442 EVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKvlhLSMNPAAEAYQQRKNQ-LEKLQAEIE 514
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
459-640 |
4.43e-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: 43.81 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 459 EEDIADKVVFLERRVLELEKDTAATGEQHSR--LRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMERE 536
Cdd:pfam02463 818 EEEQLLIEQEEKIKEEELEELALELKEEQKLekLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 537 KSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESL-----TLRLSEEQENKrRMGDRLSHERhqF 611
Cdd:pfam02463 898 EKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEkekeeNNKEEEEERNK-RLLLAKEELG--K 974
|
170 180
....*....|....*....|....*....
gi 7662234 612 QRDKEATQELIEDLRKQLEHLQLLKLEAE 640
Cdd:pfam02463 975 VNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
471-683 |
4.45e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 471 RRVLELEKDTAATGEQHSRlRQENLQLVHRANALEEQLKEQELRACEMV---LEETRRQKELLCKMEREKSIEIENLQTR 547
Cdd:PTZ00121 1188 RKAEELRKAEDARKAEAAR-KAEEERKAEEARKAEDAKKAEAVKKAEEAkkdAEEAKKAEEERNNEEIRKFEEARMAHFA 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 548 LQQLDEENSELRsctpclKANIERLEEEKQKLLDEIESLTLRLSEEQENK---RRMGDRLSHERHQFQRDKEATQELIED 624
Cdd:PTZ00121 1267 RRQAAIKAEEAR------KADELKKAEEKKKADEAKKAEEKKKADEAKKKaeeAKKADEAKKKAEEAKKKADAAKKKAEE 1340
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 7662234 625 LRKqlehlqllKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDnrNLKEQNEE 683
Cdd:PTZ00121 1341 AKK--------AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD--AAKKKAEE 1389
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
463-739 |
4.60e-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: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 463 ADKVVFLERRVLELEK---DTAATGEQHSRLRQENLQLVHRANALEEQLKE-QELRAcemVLEETRRQKELLCKMEREKS 538
Cdd:pfam05622 127 SDKVKKLEATVETYKKkleDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKaNALRG---QLETYKRQVQELHGKLSEES 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 539 IEIENLQTRLQQLDEENselrsctpclkaniERLEEEKQKLLDEIESL-----TLRLSEEQENKRRMGDRLsHERHQFQR 613
Cdd:pfam05622 204 KKADKLEFEYKKLEEKL--------------EALQKEKERLIIERDTLretneELRCAQLQQAELSQADAL-LSPSSDPG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 614 DKEATQELIEDLRKQLEHLQL----LKLEAE-QRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGqi 688
Cdd:pfam05622 269 DNLAAEIMPAEIREKLIRLQHenkmLRLGQEgSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQK-- 346
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 7662234 689 iTLSIQGAKSLFSTAFSESLAAEIssvsrDELMEAiqkQEEINfRLQDYID 739
Cdd:pfam05622 347 -ALQEQGSKAEDSSLLKQKLEEHL-----EKLHEA---QSELQ-KKKEQIE 387
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
496-684 |
4.61e-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: 42.98 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 496 QLVHRaNALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCtpclkaNIERLEEE 575
Cdd:pfam13868 27 QIAEK-KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQE------EYEEKLQE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 576 KQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELiEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYH 655
Cdd:pfam13868 100 REQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKEL-EKEEEREEDERILEYLKEKAEREEEREAEREEI 178
|
170 180
....*....|....*....|....*....
gi 7662234 656 SRARESELeQEVRRLKQDNRNLKEQNEEL 684
Cdd:pfam13868 179 EEEKEREI-ARLRAQQEKAQDEKAERDEL 206
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
472-756 |
5.48e-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: 43.50 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 472 RVLELEKDTAAtgEQHSRLRQENLQLVHRANALEEQLK-EQELRACEMVLEETRRQKELLCKMEREKSIEIE--NLQTRL 548
Cdd:TIGR00606 440 RTIELKKEILE--KKQEELKFVIKELQQLEGSSDRILElDQELRKAERELSKAEKNSLTETLKKEVKSLQNEkaDLDRKL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 549 QQLDEENSELRSCTPCLKaNIERLEEEKQKLLDEIESLTLRLSEEQ-------ENKRRMGDRLsherHQFQRDKEATQEL 621
Cdd:TIGR00606 518 RKLDQEMEQLNHHTTTRT-QMEMLTKDKMDKDEQIRKIKSRHSDELtsllgyfPNKKQLEDWL----HSKSKEINQTRDR 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 622 IEDLRKQLEhlqllKLEAEQRRGRSssmglQEYHSRARESELEQEV------RRLKQDNRNLKEQNEELNGQIITLSiqG 695
Cdd:TIGR00606 593 LAKLNKELA-----SLEQNKNHINN-----ELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLA--G 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 696 AKSLFSTAFSESLA----------------AEISSVSRD---ELMEAIQKQEEINFRLQDYIDR--IIVAIMETNPSILE 754
Cdd:TIGR00606 661 ATAVYSQFITQLTDenqsccpvcqrvfqteAELQEFISDlqsKLRLAPDKLKSTESELKKKEKRrdEMLGLAPGRQSIID 740
|
..
gi 7662234 755 VK 756
Cdd:TIGR00606 741 LK 742
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
29-209 |
6.48e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.24 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 29 AAQLAPGPAELRLGAPVGGPDPQSPGLDEPAPGAAADGGARwSAGPAPGLEGGPRDPGPSAPPPRSGPRgqlASPDAPGP 108
Cdd:PHA03307 56 VAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLA-PASPAREGSPTPPGPSSPDPPPPTPPP---ASPPPSPA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 109 GPRSEAPLPELDPLFSWTEEPEECG--PASCPESAPFRLQGSSSSHRARGEVDVFSPFPAPTAGELALEQGPGSPPQPSD 186
Cdd:PHA03307 132 PDLSEMLRPVGSPGPPPAASPPAAGasPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSS 211
|
170 180
....*....|....*....|...
gi 7662234 187 LSQTHPLPSEPVGSQEDGPRLRA 209
Cdd:PHA03307 212 PISASASSPAPAPGRSAADDAGA 234
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
520-691 |
6.56e-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: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 520 LEETRRQK-ELLCKME---REKSIEIENLQTRLQQLDEENSELRSctpclkaNIERLEEEKQKLLDEIESLTLRLSEEQe 595
Cdd:pfam07888 36 LEECLQERaELLQAQEaanRQREKEKERYKRDREQWERQRRELES-------RVAELKEELRQSREKHEELEEKYKELS- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 596 nkrRMGDRLSHERHQFQRDKEATQ----ELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQ----EYHSRARESELEQ-- 665
Cdd:pfam07888 108 ---ASSEELSEEKDALLAQRAAHEarirELEEDIKTLTQRVLERETELERMKERAKKAGAQrkeeEAERKQLQAKLQQte 184
|
170 180
....*....|....*....|....*..
gi 7662234 666 -EVRRLKQDNRNLKEQNEELNGQIITL 691
Cdd:pfam07888 185 eELRSLSKEFQELRNSLAQRDTQVLQL 211
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
572-724 |
6.80e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 572 LEEEKQKLLDEIESLTLRLSEEQENKRR-MGDRLSHERHQFQRDKEATQEL---IEDLRKQLEHLQLlKLEAEQRRGRSS 647
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTeEEEEIRRLEEQVERLEAEVEELeaeLEEKDERIERLER-ELSEARSEERRE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 648 smglqeyHSRARE-SELEQEVRRLKQDNRNLKEQNEELNGQIITLsiqgaKSLFSTAFSESLAA--EISSVSRDELMEAI 724
Cdd:COG2433 461 -------IRKDREiSRLDREIERLERELEEERERIEELKRKLERL-----KELWKLEHSGELVPvkVVEKFTKEAIRRLE 528
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
459-686 |
6.96e-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: 43.27 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 459 EEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKS 538
Cdd:pfam10174 442 EEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKS 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 539 IEIEnlqtrLQQLDEENSELRSCTPclKA-NIERLEEEKQKLLDEIESLTLRLSEEQENKRRMG---DRLSHERHQFQRD 614
Cdd:pfam10174 522 LEIA-----VEQKKEECSKLENQLK--KAhNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQaevERLLGILREVENE 594
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7662234 615 KEATQELIEDlrkqLEHLQLLKLEAEQRRGRSSSMGLQEyhSRARESELEQEVRRlKQDNRN---LKEQNEELNG 686
Cdd:pfam10174 595 KNDKDKKIAE----LESLTLRQMKEQNKKVANIKHGQQE--MKKKGAQLLEEARR-REDNLAdnsQQLQLEELMG 662
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
469-734 |
7.07e-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: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 469 LERRVLELEKDTAATGEQHSRLRQENLQLVHRANALE--------------------EQLKEQELRAcemvleETRRQKE 528
Cdd:pfam05622 12 LAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLEsgddsgtpggkkylllqkqlEQLQEENFRL------ETARDDY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 529 LLCKMEREKsiEIENLQTR----------LQQLDEENSELRSCTPCLKANIERLEEEKQKLLDeIESL--TLRLSEEqEN 596
Cdd:pfam05622 86 RIKCEELEK--EVLELQHRneeltslaeeAQALKDEMDILRESSDKVKKLEATVETYKKKLED-LGDLrrQVKLLEE-RN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 597 KRRMGDRLSHERHqfQRDKEATQELIEDLRKQLEHLQlLKLEAEQRRGRSSSMGLQEYHsrARESELEQEVRRLKQDNRN 676
Cdd:pfam05622 162 AEYMQRTLQLEEE--LKKANALRGQLETYKRQVQELH-GKLSEESKKADKLEFEYKKLE--EKLEALQKEKERLIIERDT 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7662234 677 LKEQNEEL---NGQIITLSIQGAKSLFSTAFSESLAAEISSVsrdELMEAIQKQEEINFRL 734
Cdd:pfam05622 237 LRETNEELrcaQLQQAELSQADALLSPSSDPGDNLAAEIMPA---EIREKLIRLQHENKML 294
|
|
| PRK14959 |
PRK14959 |
DNA polymerase III subunits gamma and tau; Provisional |
73-206 |
8.48e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 42.74 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 73 GPAPGLEGGPRDPGPSAPPPRSGPRGQLASPDAPGPGPRSEAPLPELdplfSWTEEPeecgpascpeSAPFRLQGssssh 152
Cdd:PRK14959 388 GPASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPAPSAAPSPRV----PWDDAP----------PAPPRSGI----- 448
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 7662234 153 rargevdvfSPFPAPTAGELALEQG-PGSPPQPSDLSQTHPLPSEPVGSQEDGPR 206
Cdd:PRK14959 449 ---------PPRPAPRMPEASPVPGaPDSVASASDAPPTLGDPSDTAEHTPSGPR 494
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
33-186 |
9.91e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.85 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 33 APGPAELRLGAPVGGPDPQSPGLDEPAPGAAADGGARWSAGPAPGLEGGPRDPGPSAPPPRSGPrgqlasPDAPGPGPRS 112
Cdd:PHA03307 293 ERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRP------PPPADPSSPR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 113 EAPLPELDPLFSWTEEPEE--------CGPASCPESAPFRLQGSSSSHRARGEVDVFSPFPAPTA-GELALEQGPGSPPQ 183
Cdd:PHA03307 367 KRPRPSRAPSSPAASAGRPtrrraraaVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYPlLTPSGEPWPGSPPP 446
|
...
gi 7662234 184 PSD 186
Cdd:PHA03307 447 PPG 449
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
4-206 |
1.00e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 4 APPASPPGSEPPGPDPEPGGPDGPGAAQLAPGPAELRLGAPVGGPDPQSPGLDEPAPGAAADGGARwSAGPAPGLEGGPR 83
Cdd:PHA03247 2603 DDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRAR-RLGRAAQASSPPQ 2681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 84 DPGPSAPPPRSGPRGQLASPDAPGPGPRSeAPLPELDPLfswteePEECGPASCPESAPfrlqgsssshrargeVDVFSP 163
Cdd:PHA03247 2682 RPRRRAARPTVGSLTSLADPPPPPPTPEP-APHALVSAT------PLPPGPAAARQASP---------------ALPAAP 2739
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 7662234 164 FPAPTAGELALEQGPGSPPQPSdLSQTHPLPSEPVGSQEDGPR 206
Cdd:PHA03247 2740 APPAVPAGPATPGGPARPARPP-TTAGPPAPAPPAAPAAGPPR 2781
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
490-697 |
1.02e-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: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 490 LRQENLQLVHRANALEEQLK-EQEL--RACEM-VLEETRRQ--KELLCKMEReksiEIENLQTRLQQLDEENSELRSCTP 563
Cdd:pfam01576 31 LEKKHQQLCEEKNALQEQLQaETELcaEAEEMrARLAARKQelEEILHELES----RLEEEEERSQQLQNEKKKMQQHIQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 564 CLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDrlshERHQFQRDKEATQELIEDLRKQL-EHLQLLKLEAEQR 642
Cdd:pfam01576 107 DLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLED----QNSKLSKERKLLEERISEFTSNLaEEEEKAKSLSKLK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 7662234 643 RGRSSSMGLQEYHSRARES---ELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAK 697
Cdd:pfam01576 183 NKHEAMISDLEERLKKEEKgrqELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
2-213 |
1.03e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.56 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 2 ASAPPASPPgseppgpDPEPGGPDGPGAAQLAPGPAELRLGAPVGGPDPQSPGLdEPAPGAAADGGARWSAGPAPGLEGG 81
Cdd:PRK12323 384 QPAPAAAAP-------AAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAP-EALAAARQASARGPGGAPAPAPAPA 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 82 PRdPGPSAPPPRSGPRGQ-LASPDAPGPGPRSEAPLPELDPLFSWTEEPEECGPASCPESAPFRLQGSSSSHRARGEVDV 160
Cdd:PRK12323 456 AA-PAAAARPAAAGPRPVaAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADP 534
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 7662234 161 FSPFPAPTAgelaleqGPGSPPQPSDLSQTHPLPSePVGSQEDGPRLRAVFDA 213
Cdd:PRK12323 535 DDAFETLAP-------APAAAPAPRAAAATEPVVA-PRPPRASASGLPDMFDG 579
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
75-217 |
1.03e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.85 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 75 APGLEGGPRDPGPSAPPPRSGPRGQLASPDAPG----------------------PGPRSEAPLPELDPLFSWTEEPEEC 132
Cdd:PHA03307 18 GEFFPRPPATPGDAADDLLSGSQGQLVSDSAELaavtvvagaaacdrfepptgppPGPGTEAPANESRSTPTWSLSTLAP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 133 GPAScPESAPFRLQGSSSSHRARGEVDVFSPFPAPTAGELALEQGPGSPPQPSDLSQTHPLPSEPVGSQEDGPRLRAVFD 212
Cdd:PHA03307 98 ASPA-REGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPL 176
|
....*
gi 7662234 213 ALDGD 217
Cdd:PHA03307 177 SSPEE 181
|
|
| Cluap1 |
pfam10234 |
Clusterin-associated protein-1; This protein is conserved from worms to humans. The protein of ... |
431-582 |
1.11e-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: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 431 KVARYLHQsgALTMEALEDPSPELMEGPEEDIADKVVFLeRRVLELEKDTAATG-------EQHSRLRQENLQLVHRANA 503
Cdd:pfam10234 86 KITSLLYN--AMKSADKEAEEEEDSTSSQFDLSSKLSDL-KAARQLASEITTKGaslydllGKEVDLREIRQQALSRPLE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 504 LEE---QLKEQeLRACEMVLEETRRQ--------KELLCKMEReKSIEIENLQTRLQQLdeenselRSCTPCLKANIERL 572
Cdd:pfam10234 163 IAEiekALKEA-IKNVAAEIEQTQKQlenlasdeANLEAKIEK-KKQELERNQKRLQTL-------QSVRPAFMDEYEKL 233
|
170
....*....|
gi 7662234 573 EEEKQKLLDE 582
Cdd:pfam10234 234 EEELQKLYEE 243
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
504-626 |
1.20e-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: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 504 LEEQLKEQE-----LRACEMVLEETRRQKEllckMEREKSIEIENLQTRLQQLDEENSEL-----RSCTPCLKANIERLE 573
Cdd:pfam02841 178 LQEFLQSKEaveeaILQTDQALTAKEKAIE----AERAKAEAAEAEQELLREKQKEEEQMmeaqeRSYQEHVKQLIEKME 253
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 7662234 574 EEKQKLLDEIESLTLRLSEEQENKRRMGdrlsherhqFQRDKEATQELIEDLR 626
Cdd:pfam02841 254 AEREQLLAEQERMLEHKLQEQEELLKEG---------FKTEAESLQKEIQDLK 297
|
|
| BCAS2 |
pfam05700 |
Breast carcinoma amplified sequence 2 (BCAS2); This family consists of several eukaryotic ... |
486-591 |
1.20e-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: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 486 QHSRLRQENLQLV--HRANA--LEEQLKEQELRACEMVLEETRRQKELLckmEREKSIEIENLQTRLQQLDEENSELRSc 561
Cdd:pfam05700 105 EHQRIRIENLELLqkYGANAwrLHNYQLEAILRRLEKELAETKEAIEEV---NRQRKNAQTAAGGELRSLEEKWKELVS- 180
|
90 100 110
....*....|....*....|....*....|
gi 7662234 562 tpclkANIErLEEEKQKLLDEIESLTLRLS 591
Cdd:pfam05700 181 -----KNLE-IEAACEALEAEILELKRQAA 204
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
540-740 |
1.24e-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: 42.36 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 540 EIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEK------QKLLDEIESL--TLRLSEEQENKRRMgDRLSHERHQF 611
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekaeryQALLKEKREYegYELLKEKEALERQK-EAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 612 QRDKEATQELIEDLRKQLEHL------------------------QLLKLEAEQRRGRSSsmgLQEYHSRAResELEQEV 667
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIeqlleelnkkikdlgeeeqlrvkeKIGELEAEIASLERS---IAEKERELE--DAEERL 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7662234 668 RRLKQDNRNLKEQNEELNGQIITLSIQgakslfstafSESLAAEISSvSRDELMEAIQKQEEINFRLQDYIDR 740
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKR----------RDKLTEEYAE-LKEELEDLRAELEEVDKEFAETRDE 386
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
507-688 |
1.43e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.60 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 507 QLK--EQELRACE-MVLEETRRQKELLCKM-EREKSI-----EIENLQTRLQQLDEENSELrsctpclKANIERLEEEK- 576
Cdd:PRK11637 48 QLKsiQQDIAAKEkSVRQQQQQRASLLAQLkKQEEAIsqasrKLRETQNTLNQLNKQIDEL-------NASIAKLEQQQa 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 577 --QKLL----------DEIESLTLRLSEEqENKRRmgdrlshERHQ--FQRDKEATQELIEDLRKQLEHLQLLKLEAEQR 642
Cdd:PRK11637 121 aqERLLaaqldaafrqGEHTGLQLILSGE-ESQRG-------ERILayFGYLNQARQETIAELKQTREELAAQKAELEEK 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 7662234 643 RGRSSS-MGLQ-------EYHSRARESELEQEVRRLKQDNRNLKE--QNE-ELNGQI 688
Cdd:PRK11637 193 QSQQKTlLYEQqaqqqklEQARNERKKTLTGLESSLQKDQQQLSElrANEsRLRDSI 249
|
|
| PHA03132 |
PHA03132 |
thymidine kinase; Provisional |
72-212 |
1.50e-03 |
|
thymidine kinase; Provisional
Pssm-ID: 222997 [Multi-domain] Cd Length: 580 Bit Score: 42.06 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 72 AGPAPGLEGGPRDPGPSAPPprSGPRGQLASPDAPGPGPRSEAPLPELDPlfswtEEPEECGPASCPEsapfrlqgSSSS 151
Cdd:PHA03132 56 PPRETGSGGGVATSTIYTVP--RPPRGPEQTLDKPDSLPASRELPPGPTP-----VPPGGFRGASSPR--------LGAD 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7662234 152 HRARGevdvFSPFPAPTAGeLALEQGPGSPPQPSDLSQTH--PLPSEPVGSQEDGPRLRAVFD 212
Cdd:PHA03132 121 STSPR----FLYQVNFPVI-LAPIGESNSSSEELSEEEEHsrPPPSESLKVKNGGKVYPKGFS 178
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
495-592 |
1.50e-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: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 495 LQLVHRANALEEQLKEqelraCEMVLEETRRQKELLCKmereksiEIENLQTRLQQLDEENSELRSctpclkaNIERLEE 574
Cdd:COG4026 124 LQNIPEYNELREELLE-----LKEKIDEIAKEKEKLTK-------ENEELESELEELREEYKKLRE-------ENSILEE 184
|
90
....*....|....*...
gi 7662234 575 EKQKLLDEIESLTLRLSE 592
Cdd:COG4026 185 EFDNIKSEYSDLKSRFEE 202
|
|
| bZIP_plant_BZIP46 |
cd14707 |
Basic leucine zipper (bZIP) domain of uncharaterized Plant BZIP transcription factors: a ... |
656-684 |
1.52e-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: 37.29 E-value: 1.52e-03
10 20 30
....*....|....*....|....*....|...
gi 7662234 656 SRAR----ESELEQEVRRLKQDNRNLKEQNEEL 684
Cdd:cd14707 16 SRARkqayTNELELEVAHLKEENARLKRQQEEL 48
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1-205 |
1.64e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 1 MASAPPASPPGSEPPGPDPEPGGPDGPGAAQLAPGPAelrlgAPVGGPDPQ---------SPGLDEPAPGAAADGGARWS 71
Cdd:PHA03247 2737 AAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPA-----APAAGPPRRltrpavaslSESRESLPSPWDPADPPAAV 2811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 72 AGPAPGLEGGPRDPGPSAPPPRSGPrgqLASPDAPGPGPRSEAPLPELDPLFSWTEEPEECGPASCPeSAPFRLQGSSSS 151
Cdd:PHA03247 2812 LAPAAALPPAASPAGPLPPPTSAQP---TAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKP-AAPARPPVRRLA 2887
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 7662234 152 hrargevdvfSPFPAPTAGELALEQ-GPGSPPQPSDLSQTHPLPSEPVGSQEDGP 205
Cdd:PHA03247 2888 ----------RPAVSRSTESFALPPdQPERPPQPQAPPPPQPQPQPPPPPQPQPP 2932
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
565-684 |
1.68e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.27 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 565 LKANIERL---EEEKQKLLDEIesltlrlseEQENKrRMGDRLsherhqfqrdKEATQELIEdLRKQLEHLQLLKleaeq 641
Cdd:pfam13851 31 LKEEIAELkkkEERNEKLMSEI---------QQENK-RLTEPL----------QKAQEEVEE-LRKQLENYEKDK----- 84
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 7662234 642 rrgrsssMGLQEyhSRARESELEQEVRRLKQDNRNLKEQNEEL 684
Cdd:pfam13851 85 -------QSLKN--LKARLKVLEKELKDLKWEHEVLEQRFEKV 118
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
570-740 |
1.73e-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: 41.65 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 570 ERLEEEKQKLLDEIESltLRLSEEQENKRRMG-DRLS-----HERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRR 643
Cdd:pfam17380 299 ERLRQEKEEKAREVER--RRKLEEAEKARQAEmDRQAaiyaeQERMAMERERELERIRQEERKRELERIRQEEIAMEISR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 644 GRS---SSMGLQEYHSRAREsELEQEVR-RLKQDNRNLKEQNEELNGQIITLSIQGAKSLFSTAFSESLAAEISSVSRDE 719
Cdd:pfam17380 377 MRElerLQMERQQKNERVRQ-ELEAARKvKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEE 455
|
170 180
....*....|....*....|....*.
gi 7662234 720 L-----MEAIQKQEEINFRLQDYIDR 740
Cdd:pfam17380 456 QerqqqVERLRQQEEERKRKKLELEK 481
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
492-642 |
1.90e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.27 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 492 QENLQLVhraNALEEQ---LKEQElRACEMVLEET----RRQKELLCKMEREksieIENLQTRLQQLDEENSELRSctpc 564
Cdd:pfam13851 22 RNNLELI---KSLKEEiaeLKKKE-ERNEKLMSEIqqenKRLTEPLQKAQEE----VEELRKQLENYEKDKQSLKN---- 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7662234 565 LKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEdlRKqlehLQLLKLEAEQR 642
Cdd:pfam13851 90 LKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLE--KK----LQALGETLEKK 161
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
469-684 |
1.92e-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: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 469 LERRVLELEKDTAATGEQHsrlrQENLQLVHraNALEEQLKEQELracemvleETRRQKELLCKMEREKSIEIENLQTRL 548
Cdd:pfam12128 327 LEDQHGAFLDADIETAAAD----QEQLPSWQ--SELENLEERLKA--------LTGKHQDVTAKYNRRRSKIKEQNNRDI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 549 QQLDEENSELRSCTPCLKANIER-LEEEKQKLLDEIESLTLRLSEEQEnkrRMGDRLSHERHQfQRDKEATQELIEDLRK 627
Cdd:pfam12128 393 AGIKDKLAKIREARDRQLAVAEDdLQALESELREQLEAGKLEFNEEEY---RLKSRLGELKLR-LNQATATPELLLQLEN 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 7662234 628 QLEHLQLLKLEAEQRRGRSSSMGLQEYHSRAREselEQEVRRLKQDNRNLKEQNEEL 684
Cdd:pfam12128 469 FDERIERAREEQEAANAEVERLQSELRQARKRR---DQASEALRQASRRLEERQSAL 522
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
470-630 |
2.48e-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: 40.11 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 470 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALeeQLKEQELRA-CEMVleetRRQKELL---CKMEREK-SIEIENL 544
Cdd:pfam17078 65 ERRLKDLEDQLSELKNSYEELTESNKQLKKRLENS--SASETTLEAeLERL----QIQYDALvdsQNEYKDHyQQEINTL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 545 QTRLQQLDEENSELrsctpcLKANIERLEEEK---QKLLDEIESLTLRLSEEQENK-RRMGDRLSHERHQFQRDK----- 615
Cdd:pfam17078 139 QESLEDLKLENEKQ------LENYQQRISSNDkdiDTKLDSYNNKFKNLDNIYVNKnNKLLTKLDSLAQLLDLPSwlnly 212
|
170
....*....|....*
gi 7662234 616 EATQELIEDLRKQLE 630
Cdd:pfam17078 213 PESRNKILEYAEKME 227
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
489-699 |
2.56e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 489 RLRQENLQLVHRANAL--EEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLK 566
Cdd:PLN02939 146 LLNQARLQALEDLEKIltEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 567 ANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGdRLSHERHQFQ---RDKEAT----QE--------LIEDLRKQLEH 631
Cdd:PLN02939 226 KELDVLKEENMLLKDDIQFLKAELIEVAETEERVF-KLEKERSLLDaslRELESKfivaQEdvsklsplQYDCWWEKVEN 304
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7662234 632 LQLLkLEAEQRRGRSSSMGLQEYHsraresELEQEVRRLKQdnrNLKEQN-EELNGQIITLSIQGAKSL 699
Cdd:PLN02939 305 LQDL-LDRATNQVEKAALVLDQNQ------DLRDKVDKLEA---SLKEANvSKFSSYKVELLQQKLKLL 363
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
2-209 |
2.61e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.31 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 2 ASAPPASPPGSEPPGPDPEPGGPDGPGAAQLAPGPAELRLGAPVGGPDPQSPGLDEPAPGAAADGGARWSagPAPGLEGG 81
Cdd:PHA03307 60 AACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPS--PAPDLSEM 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 82 PRDPGPSAPPPRSGPrgqLASPDAPGPGPRSEAPLPELDPLFSWTEEPEECgPASCPESAPFRLQGSSSSHRARGEVDVF 161
Cdd:PHA03307 138 LRPVGSPGPPPAASP---PAAGASPAAVASDAASSRQAALPLSSPEETARA-PSSPPAEPPPSTPPAAASPRPPRRSSPI 213
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 7662234 162 SPfPAPTAGELALEQGPGSPPQPSDLSQTHPLPSEPVGSQEDGPRLRA 209
Cdd:PHA03307 214 SA-SASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRP 260
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
509-672 |
2.64e-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: 41.09 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 509 KEQELRACEMVLEETRRQKELLCKMEREKSIEienlQTRLQQLDEENSELRSctpclkaniERLEEEKQKLLDEIESLTL 588
Cdd:pfam15709 328 REQEKASRDRLRAERAEMRRLEVERKRREQEE----QRRLQQEQLERAEKMR---------EELELEQQRRFEEIRLRKQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 589 RLSEEQ----ENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARESELE 664
Cdd:pfam15709 395 RLEEERqrqeEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEE 474
|
....*...
gi 7662234 665 QEVRRLKQ 672
Cdd:pfam15709 475 ERLEYQRQ 482
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
507-688 |
2.67e-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: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 507 QLKEQELRACEMVLEEtrRQKELlckmeREKSIEIENLQTRLQQLDEENSELrsctpclKANIERLEEEKQKLLDEIESL 586
Cdd:COG1579 13 QELDSELDRLEHRLKE--LPAEL-----AELEDELAALEARLEAAKTELEDL-------EKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 587 TLRLSEEQENKRRmgDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRsssmglQEYHSRARESELEQE 666
Cdd:COG1579 79 EEQLGNVRNNKEY--EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAE------LEAELEEKKAELDEE 150
|
170 180
....*....|....*....|..
gi 7662234 667 VRRLKQDNRNLKEQNEELNGQI 688
Cdd:COG1579 151 LAELEAELEELEAEREELAAKI 172
|
|
| EF-hand_6 |
pfam13405 |
EF-hand domain; |
206-235 |
2.72e-03 |
|
EF-hand domain;
Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 36.00 E-value: 2.72e-03
10 20 30
....*....|....*....|....*....|
gi 7662234 206 RLRAVFDALDGDGDGFVRIEDFIQFATVYG 235
Cdd:pfam13405 1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
535-600 |
2.84e-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: 37.55 E-value: 2.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7662234 535 REKSIEIENLQTRLQQLDEENSELrsctpclKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRM 600
Cdd:cd22887 7 QELEKRLAELEAELASLEEEIKDL-------EEELKEKNKANEILNDELIALQIENNLLEEKLRKL 65
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
535-749 |
3.20e-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: 40.82 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 535 REKSIEIENLQTRLQQLDEENSELRSCTPCLKANieRLEEEKQKLLDEIESLTLRLSEEQENKRRMgDRLSHERHQFQ-- 612
Cdd:COG5244 82 KGGLVCESKGMDKDGEIKQENHEDRIHFEESKIR--RLEETIEALKSTEKEEIVELRRENEELDKI-NLSLRERISSEep 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 613 -RDKEATQ-------ELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEyhsrARESELEQEVRRLKQDNRNLKEQNEEL 684
Cdd:COG5244 159 eLNKDGSKlsydelkEFVEESRVQVYDMVELVSDISETLNRNGSIQRSS----VRECERSNIHDVLFLVNGILDGVIDEL 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7662234 685 NGQIitlsiqgakslfstafsESLAAEISSvsrdeLMEAIQKQEEINFRLQDYIDRIIVAIMETN 749
Cdd:COG5244 235 NGEL-----------------ERLRRQLVS-----LMSSHGIEVEENSRLKATLEKFQSLELKVN 277
|
|
| bZIP |
cd14686 |
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ... |
657-688 |
3.31e-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: 36.37 E-value: 3.31e-03
10 20 30
....*....|....*....|....*....|..
gi 7662234 657 RARESELEQEVRRLKQDNRNLKEQNEELNGQI 688
Cdd:cd14686 20 KERIEELEEEVEELEEENEELKAELEELRAEV 51
|
|
| Prefoldin_2 |
pfam01920 |
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
485-586 |
3.47e-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: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 485 EQHSRLRQENLQLVHRANALEEQLKEQE--LRACEMVLEETRRQK---ELLCKMEREKSieIENLQTRLQQLDEEnselr 559
Cdd:pfam01920 2 NKFQQLQQQLQLLAQQIKQLETQLKELElaLEELELLDEDTKVYKligDVLVKQDKEEV--KEQLEERKETLEKE----- 74
|
90 100
....*....|....*....|....*..
gi 7662234 560 sctpclkanIERLEEEKQKLLDEIESL 586
Cdd:pfam01920 75 ---------IKTLEKQLEKLEKELEEL 92
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
540-719 |
3.58e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 540 EIENLQTRLQQLDEENSELrsctpclKANIERLEEEKQKLLDEIESLTLRLSEEQEnkrRMGDRLsheRHQFQRDK---- 615
Cdd:COG3883 38 ELDALQAELEELNEEYNEL-------QAELEALQAEIDKLQAEIAEAEAEIEERRE---ELGERA---RALYRSGGsvsy 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 616 ------------------------EATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMgLQEYHSRARE-----SELEQE 666
Cdd:COG3883 105 ldvllgsesfsdfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEAL-KAELEAAKAEleaqqAEQEAL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 7662234 667 VRRLKQDNRNLKEQNEELNGQIITLSIQGAKSLFSTAFSESLAAEISSVSRDE 719
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
496-730 |
3.81e-03 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 40.37 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 496 QLVHRANALEEQLKEQELRACEMVLeetRRQKELLCKMEREKSIEIENLQTRLQQL------------DEENSELRSCTP 563
Cdd:pfam03999 71 RLLHEERDPFEPKKGMSLLQKEKKL---DTQLEHLRKEKAPRLAEIKELLEQLQQLceelgeeplpllIDPLPSLEELES 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 564 CLKaNIERLEEEKQKLLDEIESLtlrlseEQENKRRMGD-----RLSHERHQFQRDKEA---TQELIEDLRKQLEHLQLL 635
Cdd:pfam03999 148 FRK-HLENLRNEKERRLEEVNEL------KKQIKLLMEEldlvpGTDFEEDLLCESEDNfclSRENIDKLRKLIKQLEEQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 636 KLEAEQR----RGRSSSM--GLQ----EYHSRARESE---------LEQEVRRLKQDNR-NLKEQNEELNGQI-----IT 690
Cdd:pfam03999 221 KAEREEKiddlREKILELwnRLQvpqeEQESFVRENNslsqdtidaLREELQRLEELKKkNIKKLIEDLRVEIeelwdKL 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 7662234 691 LSIQGAKSLFSTAFSESLA--------AEISSV-----SRDELMEAIQKQEEI 730
Cdd:pfam03999 301 FYSTEQRKRFIPFFEELYTedllelheLELKRLkeeyeSNKEILELVEKWEEL 353
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
44-197 |
3.84e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 40.82 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 44 PVGGPDPQSPGLDEPAPGAAAdggarWSagPAPGLEGGPRDPGPSAPPPRSGPRGQLASPD-APGPGPRSEA-PLPELDP 121
Cdd:PHA03378 645 VLVFPTPHQPPQVEITPYKPT-----WT--QIGHIPYQPSPTGANTMLPIQWAPGTMQPPPrAPTPMRPPAApPGRAQRP 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 122 LFSWTEEPEEC---GPASCPESAPFRL---QGSSSSHRARGEVDVFSPFPAPTAGELALEQGPGSPPQPSDLSQTHPLPS 195
Cdd:PHA03378 718 AAATGRARPPAaapGRARPPAAAPGRArppAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQ 797
|
..
gi 7662234 196 EP 197
Cdd:PHA03378 798 PP 799
|
|
| ZapB |
pfam06005 |
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
570-631 |
4.48e-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: 4.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7662234 570 ERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDR---LSHERHQFQRDKEATQELIEDLRKQLEH 631
Cdd:pfam06005 7 EQLETKIQAAVDTIALLQMENEELKEENEELKEEaneLEEENQQLKQERNQWQERIRGLLGKLDE 71
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
438-630 |
4.69e-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: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 438 QSGALTMEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTaatgEQHSR-LRQENLQLVHRANALEEQLKEQELRAC 516
Cdd:COG5185 380 DSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQI----EELQRqIEQATSSNEEVSKLLNELISELNKVMR 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 517 EMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIER-LEEEKQKLLDEIESLTLRLSEEQE 595
Cdd:COG5185 456 EADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERqLEGVRSKLDQVAESLKDFMRARGY 535
|
170 180 190
....*....|....*....|....*....|....*
gi 7662234 596 NKRRmgdrlshERHQFQRDKEATQELIEDLRKQLE 630
Cdd:COG5185 536 AHIL-------ALENLIPASELIQASNAKTDGQAA 563
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
535-631 |
5.05e-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: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 535 REKSIEI-ENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRL-SEEQENKRrmgdrlshERHQFQ 612
Cdd:pfam11559 47 RDRDLEFrESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLkTLEQKLKN--------EKEELQ 118
|
90
....*....|....*....
gi 7662234 613 RdkeaTQELIEDLRKQLEH 631
Cdd:pfam11559 119 R----LKNALQQIKTQFAH 133
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
20-185 |
5.58e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.31 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 20 EPGGPDGPGAAQLAPGPAELRLGAPVGGPDPQSPgldepapgaaadggarwSAGPAPGLEGGPRDPGpsAPPPRSGPRGQ 99
Cdd:PHA03247 2709 EPAPHALVSATPLPPGPAAARQASPALPAAPAPP-----------------AVPAGPATPGGPARPA--RPPTTAGPPAP 2769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 100 lASPDAPGPGPRSEAPLPELDPLFSWTEE-PEECGPASCPESAPFRLQGSSSSHRARGevdvfsPFPAPTAGELALEQGP 178
Cdd:PHA03247 2770 -APPAAPAAGPPRRLTRPAVASLSESRESlPSPWDPADPPAAVLAPAAALPPAASPAG------PLPPPTSAQPTAPPPP 2842
|
....*..
gi 7662234 179 GSPPQPS 185
Cdd:PHA03247 2843 PGPPPPS 2849
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
532-638 |
6.07e-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: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 532 KMERE-KSIEIENLQTRLQQLDEENSEL-RSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERH 609
Cdd:COG0542 403 RMEIDsKPEELDELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
90 100
....*....|....*....|....*....
gi 7662234 610 QFQRDKEATQELIEDLRKQLEHLQLLKLE 638
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 ... |
509-640 |
6.31e-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: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 509 KEQELRACEmvlEETRRQKELLCKMEREksieIENLQTRLQQLDEENSELrscTPCLKANIE----------RLEEEKQK 578
Cdd:pfam01576 3 QEEEMQAKE---EELQKVKERQQKAESE----LKELEKKHQQLCEEKNAL---QEQLQAETElcaeaeemraRLAARKQE 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7662234 579 LLDEIESLTLRLSEEQENKRrmgdrlsherhQFQRDKEATQELIEDLRKQLEH-------LQLLKLEAE 640
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQ-----------QLQNEKKKMQQHIQDLEEQLDEeeaarqkLQLEKVTTE 130
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
544-688 |
6.60e-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: 39.30 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 544 LQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERH------QFQRDKEA 617
Cdd:pfam15294 131 LHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGAKKDVKSNLKEISDLEEKmaalksDLEKTLNA 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7662234 618 TQELIEDLRKQL---EHlQLLKleaeqrrgrsssmgLQEYHSRArESELEQEVRRLKQdNRNLKEQNEELNGQI 688
Cdd:pfam15294 211 STALQKSLEEDLastKH-ELLK--------------VQEQLEMA-EKELEKKFQQTAA-YRNMKEMLTKKNEQI 267
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
510-733 |
7.34e-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: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 510 EQELRACEMVLEETRRQkellCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLR 589
Cdd:TIGR00618 534 EQTYAQLETSEEDVYHQ----LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDM 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 590 LSEEQENKRRMGD------RLSHERHQFQRDKEA-----TQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRA 658
Cdd:TIGR00618 610 LACEQHALLRKLQpeqdlqDVRLHLQQCSQELALkltalHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEK 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 659 RE-----SELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKslfsTAFSESLAAEISSVSRDELMEAIQKQEEINFR 733
Cdd:TIGR00618 690 EQltywkEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD----LAAREDALNQSLKELMHQARTVLKARTEAHFN 765
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
206-265 |
7.70e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 37.46 E-value: 7.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 206 RLRAVFDALDGDGDGFVRIEDFIQFAtvygAEQVKDLTKYLDPSGLGVISFEDFYQGITA 265
Cdd:COG5126 6 KLDRRFDLLDADGDGVLERDDFEALF----RRLWATLFSEADTDGDGRISREEFVAGMES 61
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
507-684 |
7.74e-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: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 507 QLKEQELRACEMVLEETRRQKELLC--KMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIE 584
Cdd:pfam01576 827 QSKESEKKLKNLEAELLQLQEDLAAseRARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTE 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 585 SLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELiEDLRKQLEhLQLLKLEAEQRRGRSSSMGLQEYHSRARESELE 664
Cdd:pfam01576 907 LLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQL-ERQNKELK-AKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLE 984
|
170 180
....*....|....*....|
gi 7662234 665 QEVRRLKQDNRNLKEQNEEL 684
Cdd:pfam01576 985 QESRERQAANKLVRRTEKKL 1004
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
49-202 |
8.30e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 39.92 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 49 DPQSPGLDEPAPGAAADGGARWSAGPAPGLEGGPRDPGPSAPPPRSGPRGQLASPDAPGPGPRSEAPLPELDPlfswtee 128
Cdd:PHA03247 2700 DPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPP------- 2772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 129 peeCGPASCPESAPFRLQGSSSSHR------ARGEVDVFSPFPAPTAGELALEQ-GPGSPPQPSDLSQTHPLPSEPVGSQ 201
Cdd:PHA03247 2773 ---AAPAAGPPRRLTRPAVASLSESreslpsPWDPADPPAAVLAPAAALPPAASpAGPLPPPTSAQPTAPPPPPGPPPPS 2849
|
.
gi 7662234 202 E 202
Cdd:PHA03247 2850 L 2850
|
|
| KLF14_N |
cd21576 |
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ... |
71-204 |
8.62e-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: 38.26 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 71 SAGPAPGleggprDPGPSAPPPrsGPRGQLASPDAPGPGPRSEAPlPELDPLFSWTEEpeecGPASCPESAPfrLQGSSS 150
Cdd:cd21576 49 SALPGPG------PPGPAWVPP--LLQVPAPSPGAGGAAPHLLAA-SVLADLRGGAGE----GSREDSGEAP--RASSGS 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 7662234 151 SHRARGEVDVFSPFPAPTAGELALeQGPGSPPQPSDLSQTHPLPSEPVGSQEDG 204
Cdd:cd21576 114 SDPARGSSPTLGSEPAPASGEDAV-SGPESSFGAPAIPSAPAAPGAPAVSGEVP 166
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
430-729 |
9.17e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.55 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 430 KKVARYLHQSGALTmEALEDPSPELMEGPEEdiadkvvflerrVLELEKDTAATGEQHSRLRQenlQLVHRANALEEQLK 509
Cdd:COG3096 347 EKIERYQEDLEELT-ERLEEQEEVVEEAAEQ------------LAEAEARLEAAEEEVDSLKS---QLADYQQALDVQQT 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 510 -----EQELRAcemvLEETRRqkelLCKMErekSIEIEN-------LQTRLQQLDEENSELR---SCTPCLKANIERLEE 574
Cdd:COG3096 411 raiqyQQAVQA----LEKARA----LCGLP---DLTPENaedylaaFRAKEQQATEEVLELEqklSVADAARRQFEKAYE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 575 EKQKLLDEIESltlrlSEEQENKRRMGDRLSHERHQFQRDKEATQELIE---DLRKQLEHLQLLKlEAEQRRGR--SSSM 649
Cdd:COG3096 480 LVCKIAGEVER-----SQAWQTARELLRRYRSQQALAQRLQQLRAQLAEleqRLRQQQNAERLLE-EFCQRIGQqlDAAE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 650 GLQEYHSR--ARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKSLFSTAFSESLAAEI--SSVSRDELMEAIQ 725
Cdd:COG3096 554 ELEELLAEleAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSgeALADSQEVTAAMQ 633
|
....
gi 7662234 726 KQEE 729
Cdd:COG3096 634 QLLE 637
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
502-737 |
9.34e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.50 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 502 NALEEQLKEQ--ELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSctpcLKANIERLEEEKQKL 579
Cdd:PRK01156 186 DYLEEKLKSSnlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSS----LEDMKNRYESEIKTA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 580 ---LDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHL--QLLKLEAEQRRGRSssmgLQEY 654
Cdd:PRK01156 262 esdLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIdaEINKYHAIIKKLSV----LQKD 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 655 HS-----RARESELEQEVRRLKQDNRN---LKEQNEELNGQIITLSIQgakslfstafSESLAAEISSVSRDELM--EAI 724
Cdd:PRK01156 338 YNdyikkKSRYDDLNNQILELEGYEMDynsYLKSIESLKKKIEEYSKN----------IERMSAFISEILKIQEIdpDAI 407
|
250
....*....|....
gi 7662234 725 QKQ-EEINFRLQDY 737
Cdd:PRK01156 408 KKElNEINVKLQDI 421
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
470-672 |
9.55e-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: 39.44 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 470 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEqLKEQELRACEMVLEETRRQ-------------KELLCKME-- 534
Cdd:pfam12128 488 ERLQSELRQARKRRDQASEALRQASRRLEERQSALDE-LELQLFPQAGTLLHFLRKEapdweqsigkvisPELLHRTDld 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 535 -------------------REKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLS---- 591
Cdd:pfam12128 567 pevwdgsvggelnlygvklDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETfart 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234 592 ---EEQENKRRMGDRLSHERHQFQRDKEATQELIEDLR-------KQLEHLQLLKLEAEQRRGRSSSMGLQEYHsRARES 661
Cdd:pfam12128 647 alkNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLnsleaqlKQLDKKHQAWLEEQKEQKREARTEKQAYW-QVVEG 725
|
250
....*....|.
gi 7662234 662 ELEQEVRRLKQ 672
Cdd:pfam12128 726 ALDAQLALLKA 736
|
|
| |
