|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
919-1193 |
9.61e-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: 79.72 E-value: 9.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 919 ILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTAST----TCEKLEKARNELQTVyEAFVQ 994
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisaLRKDLARLEAEVEQL-EERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 995 QHQAEKTERENRLKEfYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEkLELLKKAY---EASLS 1071
Cdd:TIGR02168 751 QLSKELTELEAEIEE-LEERLEEAEEE-LAEAEAEIEELEAQIEQLKEELKALREALDELRAE-LTLLNEEAanlRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1072 EIKKGHEIEKKSLEDL------LSEKQESLEKQINDLKSENDALNEKLKSEEQKRRArekanlknpqimyLEQELESLKA 1145
Cdd:TIGR02168 828 SLERRIAATERRLEDLeeqieeLSEDIESLAAEIEELEELIEELESELEALLNERAS-------------LEEALALLRS 894
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1386876317 1146 VLEIKNEKLHQQDIKLMKMEKLVDnntALVDKLKRFQQENEELKARMD 1193
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELE---ELREKLAQLELRLEGLEVRID 939
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
943-1196 |
1.67e-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: 72.40 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 943 LLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQ---------QHQAEKTERENRLKEFYTR 1013
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANeisrleqqkQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1014 EYEKL---RDTYIEEA---EKYKMQLQEQFDNLNAAHETSKLEIEASHSeKLELLKKAYEASLSEIkkgHEIEKKslEDL 1087
Cdd:TIGR02168 324 QLEELeskLDELAEELaelEEKLEELKEELESLEAELEELEAELEELES-RLEELEEQLETLRSKV---AQLELQ--IAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1088 LSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNpQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKL 1167
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA-ELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250 260
....*....|....*....|....*....
gi 1386876317 1168 VDnntALVDKLKRFQQENEELKARMDKHM 1196
Cdd:TIGR02168 477 LD---AAERELAQLQARLDSLERLQENLE 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
946-1191 |
1.14e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 946 EREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFY--TREYEKLRDTYI 1023
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYelLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1024 EEAEKyKMQLQEQFDNLNAAHETSKLEIEASHSEKLELlkkayEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLK 1103
Cdd:COG1196 306 RLEER-RRELEERLEELEEELAELEEELEELEEELEEL-----EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1104 SENDALNEKLksEEQKRRAREKANLKNPQIMyLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQ 1183
Cdd:COG1196 380 ELEELAEELL--EALRAAAELAAQLEELEEA-EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
....*...
gi 1386876317 1184 ENEELKAR 1191
Cdd:COG1196 457 EEEALLEL 464
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
921-1193 |
2.98e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 921 QLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARN---ELQTVYEAFVQQHQ 997
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIArleERRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 998 AEKTERENRLKEFYTREYEKLRDtyIEEAEKYKMQLQEQFDNLNAAhetsKLEIEASHSEKLELLKKAYEASLSEIKKgh 1077
Cdd:COG1196 323 EELAELEEELEELEEELEELEEE--LEEAEEELEEAEAELAEAEEA----LLEAEAELAEAEEELEELAEELLEALRA-- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1078 EIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKnpqimyLEQELESLKAVLEIKNEKLHQQ 1157
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE------AAEEEAELEEEEEALLELLAEL 468
|
250 260 270
....*....|....*....|....*....|....*.
gi 1386876317 1158 DIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMD 1193
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
919-1194 |
1.21e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 919 ILQLKQLLAcgntKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTvyEAFVQQHQA 998
Cdd:COG1196 224 ELEAELLLL----KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA--EEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 999 EKTEREnrlkefytREYEKLRdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAShSEKLELLKKAYEASLSEIKKGHE 1078
Cdd:COG1196 298 ARLEQD--------IARLEER---RRELEERLEELEEELAELEEELEELEEELEEL-EEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1079 IEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEE----QKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKL 1154
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEleeaEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1386876317 1155 HQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDK 1194
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
940-1195 |
2.65e-10 |
|
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: 65.08 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 940 IQHLLSEREEALKqHKTLSQELVNLRGELVTASTtcEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEfytreyeklr 1019
Cdd:TIGR02168 202 LKSLERQAEKAER-YKELKAELRELELALLVLRL--EELREELEELQEELKEAEEELEELTAELQELEEK---------- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1020 dtyIEEAEKYKMQLQEQFD-----NLNAAHETSKLEIE-ASHSEKLELLKKAYEASLSEIKkgheiEKKSLEDLLSEKQE 1093
Cdd:TIGR02168 269 ---LEELRLEVSELEEEIEelqkeLYALANEISRLEQQkQILRERLANLERQLEELEAQLE-----ELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1094 SLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKnpqimyLEQELESLK-AVLEIKNE-KLHQQDIKLMKMEKlvdnn 1171
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEE------LEEQLETLRsKVAQLELQiASLNNEIERLEARL----- 409
|
250 260
....*....|....*....|....
gi 1386876317 1172 TALVDKLKRFQQENEELKARMDKH 1195
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEA 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
916-1188 |
3.71e-10 |
|
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: 64.70 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 916 SGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEK---ARNELQTVYEAF 992
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeeeKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 993 VQQHQAEKTERENRLKEFYTReyeklrdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSE 1072
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEAR---------IEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1073 IKKghEIEKKSLED--LLSEKQES------LEKQINDLKSENDALN---EKLKSEEQKRRA-------------REKANL 1128
Cdd:TIGR02169 817 IEQ--KLNRLTLEKeyLEKEIQELqeqridLKEQIKSIEKEIENLNgkkEELEEELEELEAalrdlesrlgdlkKERDEL 894
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1129 KNpQIMYLEQELESLKAVLEIKNEKLHQQDIKLmkmEKLVDNNTALVDKLKRFQQENEEL 1188
Cdd:TIGR02169 895 EA-QLRELERKIEELEAQIEKKRKRLSELKAKL---EALEEELSEIEDPKGEDEEIPEEE 950
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
865-1187 |
8.27e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 8.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 865 RKNLFTALNAVEKSRQKNPrsLCIQPQTAPDalppEKTLeLTQYKTKCENQSGFILQLKQLLacgnTKFEALTVVIQHLL 944
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCP--VCGRELTEEH----RKEL-LEEYTAELKRIEKELKEIEEKE----RKLRKELRELEKVL 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 945 SEREEALKQHKTLSQeLVNLRGELvtASTTCEKLEKARNELQTVYEAFVQQhQAEKTERENRLKEFytREYEKLRdtyiE 1024
Cdd:PRK03918 490 KKESELIKLKELAEQ-LKELEEKL--KKYNLEELEKKAEEYEKLKEKLIKL-KGEIKSLKKELEKL--EELKKKL----A 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1025 EAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEA--SLSEIKKGHEIEKKSLEDL---LSEKQESLEKQI 1099
Cdd:PRK03918 560 ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLeeeLDKAFEELAETE 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1100 NDLKSENDALNEKLK--SEEQKRRAREKANLKNPQIMYLEQELESLKAVLE--------IKNEK--LHQQDIKLMKMEKL 1167
Cdd:PRK03918 640 KRLEELRKELEELEKkySEEEYEELREEYLELSRELAGLRAELEELEKRREeikktlekLKEELeeREKAKKELEKLEKA 719
|
330 340
....*....|....*....|
gi 1386876317 1168 VDNNTALVDKLKRFQQENEE 1187
Cdd:PRK03918 720 LERVEELREKVKKYKALLKE 739
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
976-1194 |
1.08e-09 |
|
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: 63.06 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 976 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDtyIEEAEKYKMQLQEQFDNLNAAHetSKLEIEASH 1055
Cdd:TIGR00618 127 ETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMN--LFPLDQYTQLALMEFAKKKSLH--GKAELLTLR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1056 SEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKqindLKSENDALNEKLKSEEQKRRAREKanlknpqimy 1135
Cdd:TIGR00618 203 SQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY----LTQKREAQEEQLKKQQLLKQLRAR---------- 268
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1386876317 1136 lEQELESLKAVLEIKNEKLHQQdiklMKMEKLVDNNTALVDKLKRFQQENEELKARMDK 1194
Cdd:TIGR00618 269 -IEELRAQEAVLEETQERINRA----RKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRS 322
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
994-1194 |
1.59e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 994 QQHQAEKTERENRLK----EFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYE-- 1067
Cdd:COG1196 216 RELKEELKELEAELLllklRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEll 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1068 ASLSEIKKGHEIEKKSLEDL------LSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKnpqimyLEQELE 1141
Cdd:COG1196 295 AELARLEQDIARLEERRRELeerleeLEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE------AEEALL 368
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1386876317 1142 SLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDK 1194
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
931-1194 |
5.64e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 5.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 931 TKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELvtasttcEKLEKARNELQTVyeafvqqhQAEKTERENRLKEF 1010
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL-------EELEERHELYEEA--------KAKKEELERLKKRL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1011 YTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAahETSKLEIEASHSEK-LELLKKAYE------ASLSEIKKGHEIEKKS 1083
Cdd:PRK03918 382 TGLTPEKLEKE-LEELEKAKEEIEEEISKITA--RIGELKKEIKELKKaIEELKKAKGkcpvcgRELTEEHRKELLEEYT 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1084 LE--DLLSEKQEsLEKQINDLKSENDALNEKLKSEEQKRRAREKANlknpQIMYLEQELESLKA-VLEIKNEKLHQQDIK 1160
Cdd:PRK03918 459 AElkRIEKELKE-IEEKERKLRKELRELEKVLKKESELIKLKELAE----QLKELEEKLKKYNLeELEKKAEEYEKLKEK 533
|
250 260 270
....*....|....*....|....*....|....
gi 1386876317 1161 LMKMEKLVDNNTALVDKLKRFQQENEELKARMDK 1194
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDE 567
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
900-1189 |
5.68e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.42 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 900 EKTLELTQYKTKCENQSGFILQLK-QLLACGNTKFEALTVVIQHLLSEREEALKQHKT-----------LSQELVNLRGE 967
Cdd:TIGR04523 271 EKQKELEQNNKKIKELEKQLNQLKsEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNqisqnnkiisqLNEQISQLKKE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 968 LVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTEREN--------RLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDN 1039
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNlesqindlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1040 LNAAHETSKLEIEASHSE---------KLELLKKAYEASLSEIKKGHEIEKKSLEDLLSE------KQESLEKQINDLKS 1104
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQdsvkeliikNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElkskekELKKLNEEKKELEE 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1105 ENDALNEKLKSEEQKRRAREKA-NLKNPQIMYLEQELESLKAVL---EIKNEKLH-QQDIKLMKMEK--LVDNNTALVDK 1177
Cdd:TIGR04523 511 KVKDLTKKISSLKEKIEKLESEkKEKESKISDLEDELNKDDFELkkeNLEKEIDEkNKEIEELKQTQksLKKKQEEKQEL 590
|
330
....*....|..
gi 1386876317 1178 LKRFQQENEELK 1189
Cdd:TIGR04523 591 IDQKEKEKKDLI 602
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
939-1213 |
5.89e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.52 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 939 VIQH--LLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYE---AFVQQHQAEKTERENRL----KE 1009
Cdd:pfam17380 277 IVQHqkAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDrqaAIYAEQERMAMERERELerirQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1010 FYTREYEKLRD-------TYIEEAEKYKMQLQEQFD----NLNAAHETSKLE------IEASHSEKLELLKKAYEASLSE 1072
Cdd:pfam17380 357 ERKRELERIRQeeiameiSRMRELERLQMERQQKNErvrqELEAARKVKILEeerqrkIQQQKVEMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1073 IKKGHEIEKKSLEDLLSEKQESlEKQINDLKSENDalNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLK-AVLEIKN 1151
Cdd:pfam17380 437 VRRLEEERAREMERVRLEEQER-QQQVERLRQQEE--ERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKqAMIEEER 513
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386876317 1152 E-KLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKaRMDKHMAISSFPRSRLFCKSRWR 1213
Cdd:pfam17380 514 KrKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR-RIQEQMRKATEERSRLEAMERER 575
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
976-1197 |
7.23e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 976 EKLEKARNELQTVYE--AFVQQHQAEKTERENRLKEfytreyEKlrdtyiEEAEKY-----KMQLQEQFDNLNA--AHET 1046
Cdd:TIGR02169 170 RKKEKALEELEEVEEniERLDLIIDEKRQQLERLRR------ER------EKAERYqallkEKREYEGYELLKEkeALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1047 SKLEIEASHSEKLELLKKaYEASLSEI-KKGHEIEK------KSLEDLLSEKQESLEKQINDLKSENDAL--NEKLKSEE 1117
Cdd:TIGR02169 238 QKEAIERQLASLEEELEK-LTEEISELeKRLEEIEQlleelnKKIKDLGEEEQLRVKEKIGELEAEIASLerSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1118 QKRRAREKANlknpqimyLEQELESLKAVLEIKNEKLHQQDIKLMK-MEKLVDNNTALVDKLKRFQQENEELKARMDKHM 1196
Cdd:TIGR02169 317 LEDAEERLAK--------LEAEIDKLLAEIEELEREIEEERKRRDKlTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
.
gi 1386876317 1197 A 1197
Cdd:TIGR02169 389 D 389
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
940-1101 |
1.50e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.86 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 940 IQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVY---EAFVQQHQAEKTERENRL------KEF 1010
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIkrlELEIEEVEARIKKYEEQLgnvrnnKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1011 --YTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAsHSEKLELLKKAYEASLSEIKKghEIEKksledlL 1088
Cdd:COG1579 92 eaLQKEIESLKRR-ISDLEDEILELMERIEELEEELAELEAELAE-LEAELEEKKAELDEELAELEA--ELEE------L 161
|
170
....*....|...
gi 1386876317 1089 SEKQESLEKQIND 1101
Cdd:COG1579 162 EAEREELAAKIPP 174
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
976-1197 |
1.52e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 58.01 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 976 EKLEKARNELQTVYEAFVQQH----------QAEKTERENR-LKEFYTREYEKLRDTYIEEAEKyKMQLQEQFDNLNAAH 1044
Cdd:pfam13868 61 EEKEEERKEERKRYRQELEEQieereqkrqeEYEEKLQEREqMDEIVERIQEEDQAEAEEKLEK-QRQLREEIDEFNEEQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1045 ETSK-LEIEAshsEKLELLK-KAYEASLSEIKKGHEIEKKSLE---DLLSEKQESLEKQINDLKSENDALNEKLKSEEQK 1119
Cdd:pfam13868 140 AEWKeLEKEE---EREEDERiLEYLKEKAEREEEREAEREEIEeekEREIARLRAQQEKAQDEKAERDELRAKLYQEEQE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1120 RRAREKAnlknpqimyLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKR--------FQQENEELKAR 1191
Cdd:pfam13868 217 RKERQKE---------REEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRkqaedeeiEQEEAEKRRMK 287
|
....*.
gi 1386876317 1192 MDKHMA 1197
Cdd:pfam13868 288 RLEHRR 293
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
903-1185 |
1.86e-08 |
|
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: 58.96 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 903 LELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKA- 981
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQi 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 982 ----------RNELQTVYEAFVQQH-----QAEKTERENRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHET 1046
Cdd:pfam05483 537 enleekemnlRDELESVREEFIQKGdevkcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQE 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1047 SKLEIEASHSE------------KLEL----LKKAYEASLSEIKKGHEIEKKSLEDLLSEKQES---------LEKQInD 1101
Cdd:pfam05483 617 NKALKKKGSAEnkqlnayeikvnKLELelasAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAkaiadeavkLQKEI-D 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1102 LK-----SENDALNEKLKSEEQK---RRAREKANLKNPqimylEQELESLKAVLEIKNEKLHQQdikLMKMEKLVDNNTA 1173
Cdd:pfam05483 696 KRcqhkiAEMVALMEKHKHQYDKiieERDSELGLYKNK-----EQEQSSAKAALEIELSNIKAE---LLSLKKQLEIEKE 767
|
330
....*....|..
gi 1386876317 1174 LVDKLKRFQQEN 1185
Cdd:pfam05483 768 EKEKLKMEAKEN 779
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
940-1170 |
2.01e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.99 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 940 IQHLLSEREEALKQHKTLSQELVNLRGELVTASttcEKLEKARNELQTVYEAfVQQHQAEKTERENRLKEFYtREYEKLR 1019
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQAR---SELEQLEEELEELNEQ-LQAAQAELAQAQEELESLQ-EEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1020 DTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIeASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQI 1099
Cdd:COG4372 115 EE-LEELQKERQDLEQQRKQLEAQIAELQSEI-AEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386876317 1100 ND--LKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 1170
Cdd:COG4372 193 NRnaEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
904-1149 |
2.47e-08 |
|
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: 58.53 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 904 ELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARN 983
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 984 ELQTVYEAF---VQQHQAEKTERENRLKEFyTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE 1060
Cdd:TIGR02168 863 ELEELIEELeseLEALLNERASLEEALALL-RSELEELSEE-LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1061 LLKKA---YEASLSEIKKgHEIEKKSLEDLLSEKQESLEKQINDLKSEN-DALNEklkSEEQKRRAREKANlknpQIMYL 1136
Cdd:TIGR02168 941 LQERLseeYSLTLEEAEA-LENKIEDDEEEARRRLKRLENKIKELGPVNlAAIEE---YEELKERYDFLTA----QKEDL 1012
|
250
....*....|....
gi 1386876317 1137 EQELESL-KAVLEI 1149
Cdd:TIGR02168 1013 TEAKETLeEAIEEI 1026
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
979-1201 |
4.83e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 979 EKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEK----YKMQ------------LQEQFDNLNA 1042
Cdd:COG3206 148 ELAAAVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKE-LEEAEAaleeFRQKnglvdlseeaklLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1043 AHETSKLEIEA--SHSEKLELLKKAYEASLSEIKKGHEIE--KKSLEDLLSEKQESLEK------QINDLKSENDALNEK 1112
Cdd:COG3206 227 QLAEARAELAEaeARLAALRAQLGSGPDALPELLQSPVIQqlRAQLAELEAELAELSARytpnhpDVIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1113 LKSEEQKRRAREKANLKNPQIMylEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDK-LKRFQQeneelkAR 1191
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAR--EASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESlLQRLEE------AR 378
|
250
....*....|
gi 1386876317 1192 MDKHMAISSF 1201
Cdd:COG3206 379 LAEALTVGNV 388
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
944-1136 |
4.99e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 944 LSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQA-----EKTERENRLKEFyTREYEKL 1018
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqELEALEAELAEL-PERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1019 RdtyiEEAEKYKmQLQEQFDNLNAAHETSKLEIEashsEKLELLKKAYEASLSEIKKghEIEKksledlLSEKQESLEKQ 1098
Cdd:COG4717 152 E----ERLEELR-ELEEELEELEAELAELQEELE----ELLEQLSLATEEELQDLAE--ELEE------LQQRLAELEEE 214
|
170 180 190
....*....|....*....|....*....|....*....
gi 1386876317 1099 INDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYL 1136
Cdd:COG4717 215 LEEAQEELEELEEELEQlENELEAAALEERLKEARLLLL 253
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
938-1194 |
5.34e-08 |
|
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: 57.67 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 938 VVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYeafvQQHQAEKTERENRLKEFYTREYEK 1017
Cdd:pfam02463 162 AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYY----QLKEKLELEEEYLLYLDYLKLNEE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1018 LRDTYIE----EAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQE 1093
Cdd:pfam02463 238 RIDLLQEllrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1094 SLEKQINDLKSENDAL----NEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIK------LMK 1163
Cdd:pfam02463 318 ESEKEKKKAEKELKKEkeeiEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSaaklkeEEL 397
|
250 260 270
....*....|....*....|....*....|.
gi 1386876317 1164 MEKLVDNNTALvDKLKRFQQENEELKARMDK 1194
Cdd:pfam02463 398 ELKSEEEKEAQ-LLLELARQLEDLLKEEKKE 427
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
921-1126 |
9.72e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 921 QLKQLlacgNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEK 1000
Cdd:COG4942 28 ELEQL----QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1001 TERENRLKEFYT---REYEKL------------RDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLK-- 1063
Cdd:COG4942 104 EELAELLRALYRlgrQPPLALllspedfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAel 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386876317 1064 KAYEASLSEIKKgheiEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA 1126
Cdd:COG4942 184 EEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
932-1189 |
1.03e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 932 KFEALTVVIQHLLSERE----EALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeafvqQHQAEKTERENRL 1007
Cdd:PRK03918 183 KFIKRTENIEELIKEKEkeleEVLREINEISSELPELREELEKLEKEVKELEELKEEIE--------ELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1008 KefytREYEKLRDT--YIEEAEKYKMQLQEQfdnlnaAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIekksle 1085
Cdd:PRK03918 255 R----KLEEKIRELeeRIEELKKEIEELEEK------VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1086 dlLSEKQESLEKQINDLKSENDALNEKLKSEEqkrrarekanlknpqimyleqELESLKAVLEIKNEKLHQQDIKLMKME 1165
Cdd:PRK03918 319 --LEEEINGIEERIKELEEKEERLEELKKKLK---------------------ELEKRLEELEERHELYEEAKAKKEELE 375
|
250 260
....*....|....*....|....*
gi 1386876317 1166 KLVDNNTAL-VDKLKRFQQENEELK 1189
Cdd:PRK03918 376 RLKKRLTGLtPEKLEKELEELEKAK 400
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
941-1193 |
1.60e-07 |
|
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: 55.95 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 941 QHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeafvqqhqAEKTERENRLKEFYTREYEKLRD 1020
Cdd:pfam01576 22 QKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLA-----------ARKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1021 TYIEEAEKYKMQ-----LQEQFDNLNAAHEtsKLEIEASHSE----KLELLKKAYEASLSEIKKgheiEKKSLEDLLSE- 1090
Cdd:pfam01576 91 SQQLQNEKKKMQqhiqdLEEQLDEEEAARQ--KLQLEKVTTEakikKLEEDILLLEDQNSKLSK----ERKLLEERISEf 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1091 -----KQESLEKQINDLKSENDA----LNEKLKSEEQKRRAREKANLK--------NPQIMYLEQELESLKAVLEIKNEK 1153
Cdd:pfam01576 165 tsnlaEEEEKAKSLSKLKNKHEAmisdLEERLKKEEKGRQELEKAKRKlegestdlQEQIAELQAQIAELRAQLAKKEEE 244
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1386876317 1154 LHQqdiKLMKMEKLVDNNTALVDKLKRFQQENEELKARMD 1193
Cdd:pfam01576 245 LQA---ALARLEEETAQKNNALKKIRELEAQISELQEDLE 281
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
940-1188 |
1.73e-07 |
|
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: 55.80 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 940 IQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQ---AEKTERENRLKEFYTREYE 1016
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIErlkETIIKNNSEIKDLTNQDSV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1017 KlrDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAShseKLELLKKAYE-ASLSEIKKGHEIEKKSLED---LLSEKQ 1092
Cdd:TIGR04523 452 K--ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK---QKELKSKEKElKKLNEEKKELEEKVKDLTKkisSLKEKI 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1093 ESLEKQINDLKSENDALNEKLKSEEQ---KRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVD 1169
Cdd:TIGR04523 527 EKLESEKKEKESKISDLEDELNKDDFelkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
|
250 260
....*....|....*....|...
gi 1386876317 1170 NNTALVDKLKR----FQQENEEL 1188
Cdd:TIGR04523 607 EKEKKISSLEKelekAKKENEKL 629
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
903-1189 |
1.80e-07 |
|
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: 55.80 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 903 LELTQYKTKCENQsgfILQLKQLLACGNTKFEALtvviQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKAR 982
Cdd:TIGR04523 169 EELENELNLLEKE---KLNIQKNIDKIKNKLLKL----ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 983 NELQTVYEAFVQQHQAEKTERENRLKEFYTREYEklrdtyIEEAEKYKMQLQEQFDNLNAahetsklEIEASHSEKLELL 1062
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE------LEQNNKKIKELEKQLNQLKS-------EISDLNNQKEQDW 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1063 KKAYEASLSEIKKGHEIEKKSLE------DLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANL-KNPQIMY 1135
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISqnnkiiSQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQsYKQEIKN 388
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1386876317 1136 LEQELESLKAVLEIKNEKLHQQDIKLMKMEKlvdNNTALVDKLKRFQQENEELK 1189
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQ---EKELLEKEIERLKETIIKNN 439
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
939-1188 |
4.32e-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: 54.59 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 939 VIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARnelqtvyeaFVQQHQAEKTERENRLKEF-YTREYEK 1017
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKE---------LLASRQLALQKMQSEKEQLtYWKEMLA 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1018 LRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQ--ESL 1095
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQtgAEL 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1096 EKQINDLKSENDALNE-----KLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 1170
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEdthllKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
250
....*....|....*...
gi 1386876317 1171 NTALVDKLKRFQQENEEL 1188
Cdd:TIGR00618 861 LAQLTQEQAKIIQLSDKL 878
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
976-1162 |
4.64e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 976 EKLEKARNELQTVYEAFvqqhqAEKTERENRLKEfytrEYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIE-AS 1054
Cdd:COG4717 74 KELEEELKEAEEKEEEY-----AELQEELEELEE----ELEELEAE-LEELREELEKLEKLLQLLPLYQELEALEAElAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1055 HSEKLELLKKAYEA------SLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKanl 1128
Cdd:COG4717 144 LPERLEELEERLEElreleeELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE--- 220
|
170 180 190
....*....|....*....|....*....|....*.
gi 1386876317 1129 knpQIMYLEQELESLKAVLEI--KNEKLHQQDIKLM 1162
Cdd:COG4717 221 ---ELEELEEELEQLENELEAaaLEERLKEARLLLL 253
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
982-1145 |
5.68e-07 |
|
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: 52.23 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 982 RNELQTVYEafVQQHQAEKTERENRLKEFyTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEashsEKLEL 1061
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKEL-PAELAELEDE-LAALEARLEAAKTELEDLEKEIKRLELEIE----EVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1062 LKKaYEASLSEIKK-------GHEIE-----KKSLEDLLSE---KQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA 1126
Cdd:COG1579 75 IKK-YEEQLGNVRNnkeyealQKEIEslkrrISDLEDEILElmeRIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170
....*....|....*....
gi 1386876317 1127 nlknpqimyLEQELESLKA 1145
Cdd:COG1579 154 ---------LEAELEELEA 163
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
990-1199 |
7.94e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 990 EAFVQQHQAEKTERENRLKEFYTREYEKLRDTY-------IEEAEKYKMQLQEQFDNLNAAHE-TSKLEIEASHSEKLEL 1061
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALglppdlsPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAAL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1062 LKKAYEASLSEIKKGHEIEKKSLEdlLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREkanlknpqimyLEQELE 1141
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQE--LKEELEELEEQLEELLGELEELLEALDEEELEEELEE-----------LEEELE 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876317 1142 SLKAVLEIKNEKLHQQDIKLMKMEklvdNNTALVDKLKRFQQENEELKARMDKHMAIS 1199
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLE----EDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
940-1161 |
8.23e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 940 IQHLLSEREEALKQHKTLSQELVNLR---GELVTASTTCEKLEKARNELQtvyeaFVQQHQAEKTERENRLKEfYTREYE 1016
Cdd:COG1340 73 VKELKEERDELNEKLNELREELDELRkelAELNKAGGSIDKLRKEIERLE-----WRQQTEVLSPEEEKELVE-KIKELE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1017 KLrdtyIEEAEKyKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLS---------EIKK-----GHEIEKK 1082
Cdd:COG1340 147 KE----LEKAKK-ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEmielykeadELRKeadelHKEIVEA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1083 SLE-DLLSEKQESLEKQINDLKSENDALNEKLKsEEQKRRAREKANLKNPQIMyleqelESLKavleiKNEKLHQQDIKL 1161
Cdd:COG1340 222 QEKaDELHEEIIELQKELRELRKELKKLRKKQR-ALKREKEKEELEEKAEEIF------EKLK-----KGEKLTTEELKL 289
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1023-1183 |
8.81e-07 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 52.37 E-value: 8.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1023 IEEAEKYKMQLQEQFDNLNAAHETSKleieaSHSEKLELLKKAYEASLSeiKKGHEIEKKSLEDLLSEKQESLEKQINDL 1102
Cdd:cd22656 127 LKEAKKYQDKAAKVVDKLTDFENQTE-----KDQTALETLEKALKDLLT--DEGGAIARKEIKDLQKELEKLNEEYAAKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1103 KSENDALNEKLKSEEQKRRAREK---------ANLKN------PQIMYLEQ----------ELESLKAVLEIKNEKLHQQ 1157
Cdd:cd22656 200 KAKIDELKALIADDEAKLAAALRliadltaadTDLDNllaligPAIPALEKlqgawqaiatDLDSLKDLLEDDISKIPAA 279
|
170 180
....*....|....*....|....*.
gi 1386876317 1158 DIKLMKMEKLVDNNTALVDKLKRFQQ 1183
Cdd:cd22656 280 ILAKLELEKAIEKWNELAEKADKFRQ 305
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1012-1150 |
9.00e-07 |
|
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: 52.33 E-value: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1012 TREYEKLRDtYIEEAEKYKMQLQEQFDNLNaahetSKLEIEASHSEKLE-----LLKKAYEAsLSEIKKGHEIEKKSLED 1086
Cdd:smart00787 157 KEDYKLLMK-ELELLNSIKPKLRDRKDALE-----EELRQLKQLEDELEdcdptELDRAKEK-LKKLLQEIMIKVKKLEE 229
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386876317 1087 LLSEKQEsLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKnpQIMYLEQELESLKAVLEIK 1150
Cdd:smart00787 230 LEEELQE-LESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK--EIEKLKEQLKLLQSLTGWK 290
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
913-1188 |
1.13e-06 |
|
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: 53.04 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 913 ENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEkarnELQTVYEAF 992
Cdd:COG5185 160 IIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAK----EIINIEEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 993 VQQhqaEKTERENRLKEFYTREYEKLrdtyIEEAEKYKM----QLQEQFDNLNAAHETSKLEIEaSHSEKLELLKKAYEA 1068
Cdd:COG5185 236 KGF---QDPESELEDLAQTSDKLEKL----VEQNTDLRLeklgENAESSKRLNENANNLIKQFE-NTKEKIAEYTKSIDI 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1069 SLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLE 1148
Cdd:COG5185 308 KKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIE 387
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1386876317 1149 IKNEKLHQQDIKLMKMEKlvDNNTALVDKLKRFQQENEEL 1188
Cdd:COG5185 388 STKESLDEIPQNQRGYAQ--EILATLEDTLKAADRQIEEL 425
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1034-1184 |
1.24e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 52.28 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1034 QEQFDNLNA--AHETSKLEIEASHSEKLELLKKAYEASLSEIkkghEIEKKSLEDLLSEkqesLEKQINDLKSENDALNE 1111
Cdd:PRK09039 52 DSALDRLNSqiAELADLLSLERQGNQDLQDSVANLRASLSAA----EAERSRLQALLAE----LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876317 1112 KLKSEEQ-KRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKM-EKLvdnNTALVDK---LKRFQQE 1184
Cdd:PRK09039 124 ELDSEKQvSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLgRRL---NVALAQRvqeLNRYRSE 198
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
902-1194 |
1.30e-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: 52.80 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 902 TLELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREE--ALKQHKTLS-QELVNLRGELVTASTTCEKL 978
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtKFKNNKEVElEELKKILAEDEKLLDEKKQF 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 979 EKARNELQTVYEAFV---QQHQAEKTERENRL------KEFYTREYEKLRdtyiEEAEKYKMQLQE--------QFDNLN 1041
Cdd:pfam05483 428 EKIAEELKGKEQELIfllQAREKEIHDLEIQLtaiktsEEHYLKEVEDLK----TELEKEKLKNIEltahcdklLLENKE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1042 AAHETSKLEIE-ASHSEKLELLKKAYEASLSEIKKGHEIEKKsLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKR 1120
Cdd:pfam05483 504 LTQEASDMTLElKKHQEDIINCKKQEERMLKQIENLEEKEMN-LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEV 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1121 RAREKA---------NL------KNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKME-KLVDNNTALVDKLKRFQQE 1184
Cdd:pfam05483 583 LKKEKQmkilenkcnNLkkqienKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElELASAKQKFEEIIDNYQKE 662
|
330
....*....|
gi 1386876317 1185 NEELKARMDK 1194
Cdd:pfam05483 663 IEDKKISEEK 672
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
940-1194 |
1.38e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 940 IQHLLSEREEALKQHKTLSQELVNLRGELVTAS------TTCEKLEKARNELQtvyeafvqQHQAEKTEREnrlkefyTR 1013
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkELAEQLKELEEKLK--------KYNLEELEKK-------AE 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1014 EYEKLRdtyiEEAEKYKmqlqeqfdnlnaahetSKLEIEASHSEKLELLKKAYEASLSEIKKGHEiEKKSLEDLLSEK-- 1091
Cdd:PRK03918 526 EYEKLK----EKLIKLK----------------GEIKSLKKELEKLEELKKKLAELEKKLDELEE-ELAELLKELEELgf 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1092 --QESLEKQINDL-------------KSENDALNEKLKSEEQK-RRAREKANLKNPQIMYLEQELESLKAVL------EI 1149
Cdd:PRK03918 585 esVEELEERLKELepfyneylelkdaEKELEREEKELKKLEEElDKAFEELAETEKRLEELRKELEELEKKYseeeyeEL 664
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1386876317 1150 KNEKLHQQ------DIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDK 1194
Cdd:PRK03918 665 REEYLELSrelaglRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
939-1185 |
2.58e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 939 VIQHLLSEREEALK----QHKTLSQELVNLRGELVTASTTCEKLEKARNELQTvyEAFVQQHQAEKTERE-NRLKEfYTR 1013
Cdd:TIGR04523 58 NLDKNLNKDEEKINnsnnKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS--EIKNDKEQKNKLEVElNKLEK-QKK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1014 EYEKLRDTYIEEAEKykmqLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAY--EASLSEIKKGHEIEKKSLEDL--LS 1089
Cdd:TIGR04523 135 ENKKNIDKFLTEIKK----KEKELEKLNNKYNDLKKQKEELENELNLLEKEKLniQKNIDKIKNKLLKLELLLSNLkkKI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1090 EKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA-NLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLV 1168
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEiSNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290
|
250
....*....|....*..
gi 1386876317 1169 DNNTALVDKLKRFQQEN 1185
Cdd:TIGR04523 291 NQLKSEISDLNNQKEQD 307
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
976-1156 |
3.08e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 976 EKLEKARNELQTVY--EAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLnaAHETSKLEIEA 1053
Cdd:COG4717 49 ERLEKEADELFKPQgrKPELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEEL--REELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1054 SHSEKLELLKKAyEASLSEIKKGHEIEKKSLEDL--LSEKQESLEKQINDLKSENDALNEK--LKSEEQKRRAREKANLK 1129
Cdd:COG4717 126 QLLPLYQELEAL-EAELAELPERLEELEERLEELreLEEELEELEAELAELQEELEELLEQlsLATEEELQDLAEELEEL 204
|
170 180
....*....|....*....|....*..
gi 1386876317 1130 NPQIMYLEQELESLKAVLEIKNEKLHQ 1156
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQ 231
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1005-1156 |
3.19e-06 |
|
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: 49.13 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1005 NRLKEFY---TREYEKLRDTYieEAEKYKMQLQEQfDNLNAAHETSKlEIEaSHSEKLE-LLKKAYEasLSEIKKGHEIE 1080
Cdd:pfam13851 11 NEIKNYYndiTRNNLELIKSL--KEEIAELKKKEE-RNEKLMSEIQQ-ENK-RLTEPLQkAQEEVEE--LRKQLENYEKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1081 KKSLEDLlSEKQESLEKQINDLKSENDALNEKLKSEEQKRRA------------REKANLKNpqiMYLEQELESLKAVLE 1148
Cdd:pfam13851 84 KQSLKNL-KARLKVLEKELKDLKWEHEVLEQRFEKVERERDElydkfeaaiqdvQQKTGLKN---LLLEKKLQALGETLE 159
|
....*...
gi 1386876317 1149 IKNEKLHQ 1156
Cdd:pfam13851 160 KKEAQLNE 167
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
932-1194 |
3.26e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.29 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 932 KFEALTVVIQHLLSEREEALKQHKTLSQELVNLRG---ELVtasttcEKLEKARNELQTVYEAfVQQHQAEKTERENRLK 1008
Cdd:COG1340 16 KIEELREEIEELKEKRDELNEELKELAEKRDELNAqvkELR------EEAQELREKRDELNEK-VKELKEERDELNEKLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1009 EFYT--REYEKLRDTYIEEAEKYKmQLQEQFDNLNAAHETSKLEIEAshsEKlELLKK--AYEASLSEIKKGHEIEKKSL 1084
Cdd:COG1340 89 ELREelDELRKELAELNKAGGSID-KLRKEIERLEWRQQTEVLSPEE---EK-ELVEKikELEKELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1085 EDL-----LSEKQESLEKQINDLKSENDALNEKLKSEEQKR-RAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQD 1158
Cdd:COG1340 164 ELRaelkeLRKEAEEIHKKIKELAEEAQELHEEMIELYKEAdELRKEADELHKEIVEAQEKADELHEEIIELQKELRELR 243
|
250 260 270
....*....|....*....|....*....|....*.
gi 1386876317 1159 IKLMKMEKlVDNNTALVDKLKRFQQENEELKARMDK 1194
Cdd:COG1340 244 KELKKLRK-KQRALKREKEKEELEEKAEEIFEKLKK 278
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
900-1184 |
3.31e-06 |
|
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: 51.75 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 900 EKTLELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLE 979
Cdd:pfam10174 363 KKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLE 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 980 KARNELQTVYEAFvqQHQAEKTERENRlkefytreyeklrdtyiEEAEKYKMQLQEQFDNLNAAHeTSKLEIEAShseKL 1059
Cdd:pfam10174 443 EALSEKERIIERL--KEQREREDRERL-----------------EELESLKKENKDLKEKVSALQ-PELTEKESS---LI 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1060 ELLKKAYEASLSEIKKGHEIekKSLEDLLSEKQESLEKQINDL-KSENDALNEKLKSE--EQKRRAREKANLKNPQIMYL 1136
Cdd:pfam10174 500 DLKEHASSLASSGLKKDSKL--KSLEIAVEQKKEECSKLENQLkKAHNAEEAVRTNPEinDRIRLLEQEVARYKEESGKA 577
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1386876317 1137 EQELESLKAVL-EIKNEKlHQQDIKLMKMEKL----VDNNTALVDKLKRFQQE 1184
Cdd:pfam10174 578 QAEVERLLGILrEVENEK-NDKDKKIAELESLtlrqMKEQNKKVANIKHGQQE 629
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
949-1190 |
3.68e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.51 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 949 EALKQHKTLSQELVNL--RGELVTASTTC------EKLEKARNELQTVYEAFVQQHQAEkterenrlkEFYTREYEKLrd 1020
Cdd:TIGR00618 184 MEFAKKKSLHGKAELLtlRSQLLTLCTPCmpdtyhERKQVLEKELKHLREALQQTQQSH---------AYLTQKREAQ-- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1021 tyiEEAEKYKMQLQEQ------FDNLNAAHETSKLEIE--------ASHSEKLELLKKAYEASLSEIKKgheiEKKSLED 1086
Cdd:TIGR00618 253 ---EEQLKKQQLLKQLrarieeLRAQEAVLEETQERINrarkaaplAAHIKAVTQIEQQAQRIHTELQS----KMRSRAK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1087 LLSEKQeSLEKQINDLKSENDALNEKLKSEEQKRRAREKANLK-----------------NPQIMYLEQELESLKAVLEI 1149
Cdd:TIGR00618 326 LLMKRA-AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIreiscqqhtltqhihtlQQQKTTLTQKLQSLCKELDI 404
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1386876317 1150 KNEKLHQQDIKLMKmEKLVDNNTALVDKLKRFQQENEELKA 1190
Cdd:TIGR00618 405 LQREQATIDTRTSA-FRDLQGQLAHAKKQQELQQRYAELCA 444
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
904-1195 |
3.94e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 51.01 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 904 ELTQYKTKCENQSGFILQL--------KQLLAcGNTKFEALTVVIQHLLSEREEALKQHKTLSQElvnlrGELVTASTTC 975
Cdd:pfam06160 108 ELDELLESEEKNREEVEELkdkyrelrKTLLA-NRFSYGPAIDELEKQLAEIEEEFSQFEELTES-----GDYLEAREVL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 976 EKLEKARNELQTVYEAFVQQHQaekterenRLKEFYTREYEKLRDTYIE-EAEKYK---MQLQEQFDNLNAAHETS---- 1047
Cdd:pfam06160 182 EKLEEETDALEELMEDIPPLYE--------ELKTELPDQLEELKEGYREmEEEGYAlehLNVDKEIQQLEEQLEENlall 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1048 -KLEIEAShSEKLELLKKA----YEASLSEIKKGHEIEKKS--LEDLLS---------------------------EKQE 1093
Cdd:pfam06160 254 eNLELDEA-EEALEEIEERidqlYDLLEKEVDAKKYVEKNLpeIEDYLEhaeeqnkelkeelervqqsytlnenelERVR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1094 SLEKQINDLKSENDALNEKLKSEEQkrrarekanlknPQIMYLEQELESLKAVLEIKNEklhQQDIK--LMKMEKlvDNN 1171
Cdd:pfam06160 333 GLEKQLEELEKRYDEIVERLEEKEV------------AYSELQEELEEILEQLEEIEEE---QEEFKesLQSLRK--DEL 395
|
330 340
....*....|....*....|....
gi 1386876317 1172 TALvDKLKRFQQENEELKARMDKH 1195
Cdd:pfam06160 396 EAR-EKLDEFKLELREIKRLVEKS 418
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
978-1197 |
5.67e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 49.92 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 978 LEKARNELQTVYEAFVQQHQAEkterENRLKEFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHET----------- 1046
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAE----PSRLYSLYEKEIEDLRRQ-LDTLTVERARLQLELDNLRLAAEDfrqkyedelnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1047 --------------------SKLEIEA---SHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQEsLEKQINDLK 1103
Cdd:pfam00038 98 rtsaendlvglrkdldeatlARVDLEAkieSLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLD-LTSALAEIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1104 SENDALNEKLKSE--------------------EQKRRAREKANLKNPQIMYLEQELESL---KAVLEIKNEKLHQQDIK 1160
Cdd:pfam00038 177 AQYEEIAAKNREEaeewyqskleelqqaaarngDALRSAKEEITELRRTIQSLEIELQSLkkqKASLERQLAETEERYEL 256
|
250 260 270
....*....|....*....|....*....|....*....
gi 1386876317 1161 LMKM--EKLVDNNTALVDKLKRFQQENEELKARMDKHMA 1197
Cdd:pfam00038 257 QLADyqELISELEAELQETRQEMARQLREYQELLNVKLA 295
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
955-1193 |
6.56e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 955 KTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFvqQHQAEKTERENRLKEfYTREYEKLRDTY--IEEAEKYKMQ 1032
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREAL--QRLAEYSWDEIDVAS-AEREIAELEAELerLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1033 LQEQFDNLNAAHETSKLEIEASHSEK---------LELLKKAYEASLSEIKKGHEIEKKSL--EDLLSEKQESLEKQI-N 1100
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIgrlekeleqAEEELDELQDRLEAAEDLARLELRALleERFAAALGDAVERELrE 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1101 DLKSENDALNEKLKSEEQK-RRAREKANLKNPQIMY-LEQELESLKAVLE----IKNEKL--HQQDIKLMKMEKLVDNNT 1172
Cdd:COG4913 770 NLEERIDALRARLNRAEEElERAMRAFNREWPAETAdLDADLESLPEYLAlldrLEEDGLpeYEERFKELLNENSIEFVA 849
|
250 260
....*....|....*....|.
gi 1386876317 1173 ALVDKLKRfqqENEELKARMD 1193
Cdd:COG4913 850 DLLSKLRR---AIREIKERID 867
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
946-1194 |
6.76e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.28 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 946 EREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQA---EKTERENRLKEF-----------Y 1011
Cdd:pfam07888 67 DREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDAllaQRAAHEARIRELeediktltqrvL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1012 TREYEKLRDTyiEEAEKYKMQLQEQfdnlNAAHETSKLEIEASHSEKLELLKKAYEAslseikKGHEIEKKSLEDLLSEK 1091
Cdd:pfam07888 147 ERETELERMK--ERAKKAGAQRKEE----EAERKQLQAKLQQTEEELRSLSKEFQEL------RNSLAQRDTQVLQLQDT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1092 QESLEKQINDlKSENDALNEKLKseEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKME-KLVDN 1170
Cdd:pfam07888 215 ITTLTQKLTT-AHRKEAENEALL--EELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTlQLADA 291
|
250 260
....*....|....*....|....*.
gi 1386876317 1171 NTALVDKLKRFQQENEELK--ARMDK 1194
Cdd:pfam07888 292 SLALREGRARWAQERETLQqsAEADK 317
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
930-1194 |
7.48e-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: 50.40 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 930 NTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVyeafVQQHQAEKTERENRLKE 1009
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK----IEKLESEKKEKESKISD 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1010 fytREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKlEIEASHSEKLELLKKaYEASLSEIKKghEIEKKSledlls 1089
Cdd:TIGR04523 543 ---LEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQK-SLKKKQEEKQELIDQ-KEKEKKDLIK--EIEEKE------ 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1090 EKQESLEKQINDLKSENDALNEKLKSEEQKrrarekanlKNPQIMYLEQELESLKAVLEIKNE---------KLHQQDIK 1160
Cdd:TIGR04523 610 KKISSLEKELEKAKKENEKLSSIIKNIKSK---------KNKLKQEVKQIKETIKEIRNKWPEiikkikeskTKIDDIIE 680
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1386876317 1161 LMK----------------------MEKLVDNNTALVDKLKRFQQENEELKARMDK 1194
Cdd:TIGR04523 681 LMKdwlkelslhykkyitrmirikdLPKLEEKYKEIEKELKKLDEFSKELENIIKN 736
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
904-1191 |
8.04e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 904 ELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARN 983
Cdd:COG4372 46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 984 ELQT---VYEAFVQQHQAEKTERENRLKEFYTREYEKLRDtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE 1060
Cdd:COG4372 126 DLEQqrkQLEAQIAELQSEIAEREEELKELEEQLESLQEE--LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1061 LLKKAYEASLSEIKKGHEIEKKSLE---DLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLE 1137
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEaklGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1386876317 1138 QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKAR 1191
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLA 337
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
871-1102 |
9.82e-06 |
|
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: 50.34 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 871 ALNAVEKSRQknprsLCIQPQTAPDALPPEktleLTQYKTKCENQSGFILQLKQLLACGN---TKFEALTVVIQHLLSE- 946
Cdd:COG3096 418 AVQALEKARA-----LCGLPDLTPENAEDY----LAAFRAKEQQATEEVLELEQKLSVADaarRQFEKAYELVCKIAGEv 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 947 -REEA-------LKQH---KTLSQELVNLRGELVTAsttcEKLEKARNELQTVYEAFVQQHQAEKTERENrLKEFYTREY 1015
Cdd:COG3096 489 eRSQAwqtarelLRRYrsqQALAQRLQQLRAQLAEL----EQRLRQQQNAERLLEEFCQRIGQQLDAAEE-LEELLAELE 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1016 EKLRD--TYIEEAEKYKMQLQEQFDNLNAAHEtsKLEIEASH----SEKLELLKKAYEASL---SEIKKG------HEIE 1080
Cdd:COG3096 564 AQLEEleEQAAEAVEQRSELRQQLEQLRARIK--ELAARAPAwlaaQDALERLREQSGEALadsQEVTAAmqqlleRERE 641
|
250 260
....*....|....*....|..
gi 1386876317 1081 KKSLEDLLSEKQESLEKQINDL 1102
Cdd:COG3096 642 ATVERDELAARKQALESQIERL 663
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
935-1193 |
1.55e-05 |
|
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: 48.99 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 935 ALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVyeafVQQHQAEKTERENRLKEFyTRE 1014
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR----IRALEQELAALEAELAEL-EKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1015 YEKLRdtyiEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKA-YEASLSEikkgheiEKKSLEDLLSEKQE 1093
Cdd:COG4942 92 IAELR----AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqYLKYLAP-------ARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1094 SLEKQINDLKSENDALNEKLKSEEQKRRArekanlknpqimyLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTA 1173
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAA-------------LEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
250 260
....*....|....*....|
gi 1386876317 1174 LVDKLKRFQQENEELKARMD 1193
Cdd:COG4942 228 LIARLEAEAAAAAERTPAAG 247
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
1013-1179 |
1.59e-05 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 46.07 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1013 REYEKLRDTYIEEAEKYKM----QLQEQFDNLNAAHETSKLEIEAShSEKLELLKKAYEASlSEIKKGHEIEKKSLEDLL 1088
Cdd:pfam09744 10 KEFERLIDRYGEDVVKGLMpkvvNVLELLESLASRNQEHNVELEEL-REDNEQLETQYERE-KALRKRAEEELEEIEDQW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1089 SEKQESLEKQINDLKSENDALneklkseEQKRRARekanlknpqimyleqeLESLKAVLEIKNEKLHQQDIKLMKmeKLV 1168
Cdd:pfam09744 88 EQETKDLLSQVESLEEENRRL-------EADHVSR----------------LEEKEAELKKEYSKLHERETEVLR--KLK 142
|
170
....*....|.
gi 1386876317 1169 DnntaLVDKLK 1179
Cdd:pfam09744 143 E----VVDRQR 149
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
904-1193 |
1.63e-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: 49.35 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 904 ELTQYKTKCENQSGFILQLKQLL-----ACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASttcEKL 978
Cdd:pfam15921 171 QIEQLRKMMLSHEGVLQEIRSILvdfeeASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVE---DQL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 979 EKARNELQTVYEAFVQQHQaektereNRLKEFYTrEYEKLRDTYIEEAEKYKMQ----------LQEQFDNLNAAHETSK 1048
Cdd:pfam15921 248 EALKSESQNKIELLLQQHQ-------DRIEQLIS-EHEVEITGLTEKASSARSQansiqsqleiIQEQARNQNSMYMRQL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1049 LEIEASHSE---KLELLKKAYEASLSEIKK-----GHEI------------EKKSLEDLLS---------EKQESLEKQ- 1098
Cdd:pfam15921 320 SDLESTVSQlrsELREAKRMYEDKIEELEKqlvlaNSELtearterdqfsqESGNLDDQLQklladlhkrEKELSLEKEq 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1099 --------------INDLKSEND----------ALNEKLKSEEQKRRAREKANLKNP-----QIMYLEQELESLKAVLEI 1149
Cdd:pfam15921 400 nkrlwdrdtgnsitIDHLRRELDdrnmevqrleALLKAMKSECQGQMERQMAAIQGKnesleKVSSLTAQLESTKEMLRK 479
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1386876317 1150 KNEKLHQQDIKLMKMEKLV-DNNTALVDKLKRFQQENEE---LKARMD 1193
Cdd:pfam15921 480 VVEELTAKKMTLESSERTVsDLTASLQEKERAIEATNAEitkLRSRVD 527
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
1048-1193 |
2.20e-05 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 45.76 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1048 KLEIEASHSEKLELLKKAYEASLSEIKKGHEIEkksledllsekqeSLEKQINDLKSENDALNEKLKseEQKRRAREKAN 1127
Cdd:pfam12718 6 KLEAENAQERAEELEEKVKELEQENLEKEQEIK-------------SLTHKNQQLEEEVEKLEEQLK--EAKEKAEESEK 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386876317 1128 LK------NPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKlvdnntalvdKLKRFQQENEELKARMD 1193
Cdd:pfam12718 71 LKtnnenlTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLER----------KVQALEQERDEWEKKYE 132
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
976-1166 |
2.32e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 976 EKLEKARNELQTVYEAFVQQHQAE--KTERENRLKEFYTREYEKLRDTY-----IEEAEKYK---MQLQEQFDNLNAAHE 1045
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEeaKKAEEAKIKAEELKKAEEEKKKVeqlkkKEAEEKKKaeeLKKAEEENKIKAAEE 1666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1046 TSKLEIEASHSEKL------------ELLKKAYEA-SLSEIKKGHEIEKKSLEDLLSEKQESLEKqINDLKSENDalNEK 1112
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAkkaeedekkaaeALKKEAEEAkKAEELKKKEAEEKKKAEELKKAEEENKIK-AEEAKKEAE--EDK 1743
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1386876317 1113 LKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIK-LMKMEK 1166
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKrRMEVDK 1798
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
942-1184 |
2.89e-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: 48.58 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 942 HLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVyeafVQQHQAEKTERENRLKEfyTREYEKLRDT 1021
Cdd:pfam05557 10 RLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKR----IRLLEKREAEAEEALRE--QAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1022 YIEEAEKykmQLQEQFDNLNAAHETS---KLEIEA----SHSEKLELLKKAYEasLSEIKKGHEIEKKSLEDLlSEKQES 1094
Cdd:pfam05557 84 YLEALNK---KLNEKESQLADAREVIsclKNELSElrrqIQRAELELQSTNSE--LEELQERLDLLKAKASEA-EQLRQN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1095 LEKQINDLKSENDALNE---KLKSEEQKRRAREKANLKNPQIMYLEQELE----------SLKAVLEIKNEKLHQQDIKL 1161
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKElefEIQSQEQDSEIVKNSKSELARIPELEKELErlrehnkhlnENIENKLLLKEEVEDLKRKL 237
|
250 260
....*....|....*....|...
gi 1386876317 1162 MKMEKLVDNNTALVDKLKRFQQE 1184
Cdd:pfam05557 238 EREEKYREEAATLELEKEKLEQE 260
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
930-1193 |
3.13e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 930 NTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKarnELQTVYEAF---------VQQHQAEK 1000
Cdd:PRK02224 341 NEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE---EIEELRERFgdapvdlgnAEDFLEEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1001 TERENRLKEFYTR---EYEKLRDTyIEEAEkykmQLQ-------------------------EQFDNLNAAHETSKLEIE 1052
Cdd:PRK02224 418 REERDELREREAEleaTLRTARER-VEEAE----ALLeagkcpecgqpvegsphvetieedrERVEELEAELEDLEEEVE 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1053 AShSEKLELLKKAYEASlSEIKKGHEiEKKSLEDLLSEKQESLE----------KQINDLKSENDALNEKL-KSEEQKRR 1121
Cdd:PRK02224 493 EV-EERLERAEDLVEAE-DRIERLEE-RREDLEELIAERRETIEekreraeelrERAAELEAEAEEKREAAaEAEEEAEE 569
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386876317 1122 AREKANLKNPQIMYLEQELESLKAVLEIkneklhqqdikLMKMEKLVDNNTALVDKLKRFQQENEELKARMD 1193
Cdd:PRK02224 570 AREEVAELNSKLAELKERIESLERIRTL-----------LAAIADAEDEIERLREKREALAELNDERRERLA 630
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
992-1157 |
3.31e-05 |
|
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: 46.66 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 992 FVQQHQAEKTERENrLKEFYTREYEKLRDTyieeaEKYKMQLQEQFDNLNAAHETSKLE------IEASHSEKLELLKKA 1065
Cdd:pfam17078 43 FLENLASLKHENDN-LSSMLNRKERRLKDL-----EDQLSELKNSYEELTESNKQLKKRlenssaSETTLEAELERLQIQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1066 YEASLSEIK--KGH---EIE--KKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREkaNLKNPQIMYLEQ 1138
Cdd:pfam17078 117 YDALVDSQNeyKDHyqqEINtlQESLEDLKLENEKQLENYQQRISSNDKDIDTKLDSYNNKFKNLD--NIYVNKNNKLLT 194
|
170 180
....*....|....*....|
gi 1386876317 1139 ELESLKAVLEIKN-EKLHQQ 1157
Cdd:pfam17078 195 KLDSLAQLLDLPSwLNLYPE 214
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
976-1194 |
3.36e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 976 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEiEASH 1055
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE-EAKK 1571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1056 SE--------KLELLKKAYEASLSEIKKGHEIEKKSLEDLLSE------------KQESLEKQINDLKSENDalnEKLKS 1115
Cdd:PTZ00121 1572 AEedknmalrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaeeakikaeelkKAEEEKKKVEQLKKKEA---EEKKK 1648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1116 EEQKRRAREKANLKNPQIMYLEQE----LESLKAVLEIKN---EKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEEL 1188
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEdkkkAEEAKKAEEDEKkaaEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728
|
....*.
gi 1386876317 1189 KARMDK 1194
Cdd:PTZ00121 1729 KIKAEE 1734
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1013-1194 |
3.77e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1013 REYEKLRDTYIEEAEKykmqlqeqfdnlNAAHETSKLEIEAShsEKLELLKKAYEASLSEIKKghEIEKksLEDLLSEKQ 1092
Cdd:PRK12704 34 KEAEEEAKRILEEAKK------------EAEAIKKEALLEAK--EEIHKLRNEFEKELRERRN--ELQK--LEKRLLQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1093 ESLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpqimyLEQELESLKAVLEIKNEK---LHQQDIKLMKMEKLVD 1169
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKELEQKQQELEK----------KEEELEELIEEQLQELERisgLTAEEAKEILLEKVEE 165
|
170 180
....*....|....*....|....*
gi 1386876317 1170 NNTAlvDKLKRFQQENEELKARMDK 1194
Cdd:PRK12704 166 EARH--EAAVLIKEIEEEAKEEADK 188
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1057-1194 |
3.92e-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: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1057 EKLELLKK--AYEASLSEIK---KGHEIEKKSLEDLLSEKQESLEK---QINDLKSENDALNEKLKSEEQKR-RAREK-A 1126
Cdd:COG1579 4 EDLRALLDlqELDSELDRLEhrlKELPAELAELEDELAALEARLEAaktELEDLEKEIKRLELEIEEVEARIkKYEEQlG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1127 NLKNP-QIMYLEQELESLKAVLEIKNEKLhqqdIKLM-KMEKLVDNNTALVDKLKRFQQENEELKARMDK 1194
Cdd:COG1579 84 NVRNNkEYEALQKEIESLKRRISDLEDEI----LELMeRIEELEEELAELEAELAELEAELEEKKAELDE 149
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1023-1197 |
4.31e-05 |
|
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: 47.45 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1023 IEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEkLELLKKAYEASLSEIKKgheiekksledlLSEKQESLEKQINDL 1102
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ-LAALERRIAALARRIRA------------LEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1103 KSENDALNEKLKSEEQKRRAREKANLKNPQIMYLE------------QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 1170
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllspedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180
....*....|....*....|....*..
gi 1386876317 1171 NTALVDKLKRFQQENEELKARMDKHMA 1197
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKA 195
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
948-1120 |
4.44e-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: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 948 EEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKefytREyeklrdtyIEEAE 1027
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLE----RE--------IERLE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1028 KYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEikkgheiekKSLEDLLSEKQESLEKQINDLKSEND 1107
Cdd:COG4913 352 RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL---------EEELEALEEALAEAEAALRDLRRELR 422
|
170
....*....|...
gi 1386876317 1108 ALNEKLKSEEQKR 1120
Cdd:COG4913 423 ELEAEIASLERRK 435
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
904-1195 |
4.87e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.52 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 904 ELTQYKTKCENQSGFILQL--------KQLLAcGNTKFEALTVVIQHLLSEREEALKQHKTLSQElvnlrGELVTASttc 975
Cdd:PRK04778 127 ELQELLESEEKNREEVEQLkdlyrelrKSLLA-NRFSFGPALDELEKQLENLEEEFSQFVELTES-----GDYVEAR--- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 976 EKLEKARNELQTVyeafvqQHQAEK-----TERENRLKEfytrEYEKLRDTYIE-EAEKYK---MQLQEQFDNLNAAHET 1046
Cdd:PRK04778 198 EILDQLEEELAAL------EQIMEEipellKELQTELPD----QLQELKAGYRElVEEGYHldhLDIEKEIQDLKEQIDE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1047 -----SKLEIEAShSEKLELLKKA----YEASLSEIKKGHEIEKKS--LEDLLS-------------------------- 1089
Cdd:PRK04778 268 nlallEELDLDEA-EEKNEEIQERidqlYDILEREVKARKYVEKNSdtLPDFLEhakeqnkelkeeidrvkqsytlnese 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1090 -EKQESLEKQINDLKSENDALNEKLksEEQKRRAREkanlknpqimyLEQELESLKAVL-EIKNEklhQQDIK--LMKME 1165
Cdd:PRK04778 347 lESVRQLEKQLESLEKQYDEITERI--AEQEIAYSE-----------LQEELEEILKQLeEIEKE---QEKLSemLQGLR 410
|
330 340 350
....*....|....*....|....*....|
gi 1386876317 1166 KlvDNNTALvDKLKRFQQENEELKARMDKH 1195
Cdd:PRK04778 411 K--DELEAR-EKLERYRNKLHEIKRYLEKS 437
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1006-1201 |
5.10e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1006 RLKEFYTREYEKLRDTYIEEAEKykMQLqeqFDNLNAAHETSKLE-IEAshsekleLLKKAYEASLSEIKKG----HEIE 1080
Cdd:COG4717 2 KIKELEIYGFGKFRDRTIEFSPG--LNV---IYGPNEAGKSTLLAfIRA-------MLLERLEKEADELFKPqgrkPELN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1081 KKSLEDLLSEKQE--SLEKQINDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYLE--QELESLKAVLEIKNEKLH 1155
Cdd:COG4717 70 LKELKELEEELKEaeEKEEEYAELQEELEELEEELEElEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1386876317 1156 QQDIKLMKMEklvdnntALVDKLKRFQQENEELKARMDKHMAISSF 1201
Cdd:COG4717 150 ELEERLEELR-------ELEEELEELEAELAELQEELEELLEQLSL 188
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
993-1197 |
5.70e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 46.18 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 993 VQQHQAEKTERENRLKEFyTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKlEIEASHSEKLELLKKAYEASlSE 1072
Cdd:pfam00261 3 MQQIKEELDEAEERLKEA-MKKLEEAEKR-AEKAEAEVAALNRRIQLLEEELERTE-ERLAEALEKLEEAEKAADES-ER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1073 IKKGheIEKKSLEDllSEKQESLEKQINDLKSENDALNEKLKSEEQK--------RRAREKANLKNPQIMYLEQEL---- 1140
Cdd:pfam00261 79 GRKV--LENRALKD--EEKMEILEAQLKEAKEIAEEADRKYEEVARKlvvvegdlERAEERAELAESKIVELEEELkvvg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1141 ESLKAvLEIKNEKLHQQDIK-------------------------LMKMEKLVDnntALVDKLKRFQQENEELKARMDKH 1195
Cdd:pfam00261 155 NNLKS-LEASEEKASEREDKyeeqirflteklkeaetraefaersVQKLEKEVD---RLEDELEAEKEKYKAISEELDQT 230
|
..
gi 1386876317 1196 MA 1197
Cdd:pfam00261 231 LA 232
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
1055-1197 |
8.42e-05 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 43.70 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1055 HSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEK-QINDLKsendALNEKLKSEEQKRRAREKANLKNpQI 1133
Cdd:pfam12474 1 HQLQKEQQKDRFEQERQQLKKRYEKELEQLERQQKQQIEKLEQrQTQELR----RLPKRIRAEQKKRLKMFRESLKQ-EK 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386876317 1134 MYLEQELESLKavleikneKLHQQDIKLMKMEKLvdnntalvdKLKRFQQENEELKARMDKHMA 1197
Cdd:pfam12474 76 KELKQEVEKLP--------KFQRKEAKRQRKEEL---------ELEQKHEELEFLQAQSEALER 122
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
910-1161 |
1.11e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 910 TKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQhktLSQELVNLRGELVtasttcEKLEKARNELQTVY 989
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAE---LNQLLRTLDDQWK------EKRDELNGELSAAD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 990 EAfVQQHQAEKTERENRLKEFYTREYEKLR---------DTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE 1060
Cdd:pfam12128 315 AA-VAKDRSELEALEDQHGAFLDADIETAAadqeqlpswQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIA 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1061 LLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSE--------------EQKR------ 1120
Cdd:pfam12128 394 GIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELklrlnqatatpellLQLEnfderi 473
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1386876317 1121 -RAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKL 1161
Cdd:pfam12128 474 eRAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRL 515
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
955-1199 |
1.14e-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: 46.71 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 955 KTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFV--QQHQ------------------AE-------------KT 1001
Cdd:pfam01576 548 KRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLvdLDHQrqlvsnlekkqkkfdqmlAEekaisaryaeerdRA 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1002 ERENRLKEF----YTREYEKLRDTyIEEAEKYKMQLQEQFDNL--------NAAH--ETSKLEIEASHSE---KLELL-- 1062
Cdd:pfam01576 628 EAEAREKETralsLARALEEALEA-KEELERTNKQLRAEMEDLvsskddvgKNVHelERSKRALEQQVEEmktQLEELed 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1063 --------KKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDalneklksEEQKRRAREKANLKNpqim 1134
Cdd:pfam01576 707 elqatedaKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELE--------DERKQRAQAVAAKKK---- 774
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1386876317 1135 yLEQELESLKAVLEIKNeKLHQQDIKLMKmeklvdnntALVDKLKRFQQENEELKARMDKHMAIS 1199
Cdd:pfam01576 775 -LELDLKELEAQIDAAN-KGREEAVKQLK---------KLQAQMKDLQRELEEARASRDEILAQS 828
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
979-1125 |
1.19e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 979 EKARNELQTVYEAFVQQHQAEKTEREnRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEiEASHSEK 1058
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEE-RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEE 1300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1386876317 1059 L----ELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREK 1125
Cdd:PTZ00121 1301 KkkadEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
941-1157 |
1.30e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 941 QHLLSEREEALKQHKTLSQELVNLRgelvtasttcEKLEKARNELQtvyeAFVQQH-----QAEKTERENRLKEfYTREY 1015
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELR----------KELEEAEAALE----EFRQKNglvdlSEEAKLLLQQLSE-LESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1016 EKLRDTYIEEAEKYKmQLQEQFD-NLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGH----EIEKKsLEDLLSE 1090
Cdd:COG3206 229 AEARAELAEAEARLA-ALRAQLGsGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdviALRAQ-IAALRAQ 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876317 1091 KQESLEKQINDLKSENDALNEKLKS-EEQKRRAREKANlKNPQimyLEQELESLKAVLEIkNEKLHQQ 1157
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASlQAQLAQLEARLA-ELPE---LEAELRRLEREVEV-ARELYES 369
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
947-1200 |
1.51e-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: 46.32 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 947 REEALKQHKTLSQELVNLRGELV-TASTTC-------------EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEfyT 1012
Cdd:pfam01576 287 RNKAEKQRRDLGEELEALKTELEdTLDTTAaqqelrskreqevTELKKALEEETRSHEAQLQEMRQKHTQALEELTE--Q 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1013 REYEKLRDTYIEEA----EKYKMQLQEQFDNLNAA-----HETSKL-----EIEASHSE----KLELLKKAYE------- 1067
Cdd:pfam01576 365 LEQAKRNKANLEKAkqalESENAELQAELRTLQQAkqdseHKRKKLegqlqELQARLSEserqRAELAEKLSKlqseles 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1068 --ASLSEI-KKGHEIEKK--SLEDLLSEKQE----------SLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpQ 1132
Cdd:pfam01576 445 vsSLLNEAeGKNIKLSKDvsSLESQLQDTQEllqeetrqklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVER------Q 518
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1386876317 1133 IMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN-------NTALVDKL----KRFQQENEELKARMDKHMAISS 1200
Cdd:pfam01576 519 LSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEAltqqleeKAAAYDKLektkNRLQQELDDLLVDLDHQRQLVS 597
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
1006-1149 |
1.57e-04 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 45.01 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1006 RLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSE--KLELLKKAYEASLSEIKKGHEIEK-- 1081
Cdd:PRK06669 26 RFKVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEeaKEELLKKTDEASSIIEKLQMQIEReq 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386876317 1082 -KSLEDLLSEKQESLEKQIND--LKSENDALNEKLKSEEQKRRAREKANLK-NPQIMYLEQELESLkaVLEI 1149
Cdd:PRK06669 106 eEWEEELERLIEEAKAEGYEEgyEKGREEGLEEVRELIEQLNKIIEKLIKKrEEILESSEEEIVEL--ALDI 175
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
997-1190 |
1.58e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 997 QAEKTERenrlkefytreYEKLRdtyiEEAEKYKMQLQ-EQFDNLNAAHETSKLEIEAshsekLELLKKAYEASLSEIKK 1075
Cdd:COG1196 208 QAEKAER-----------YRELK----EELKELEAELLlLKLRELEAELEELEAELEE-----LEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1076 GHEIEKKSLEDLlsekqeslEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpQIMYLEQELESLKAVLEIKNEKL- 1154
Cdd:COG1196 268 ELEELRLELEEL--------ELELEEAQAEEYELLAELARLEQDIARLEE------RRRELEERLEELEEELAELEEELe 333
|
170 180 190
....*....|....*....|....*....|....*..
gi 1386876317 1155 -HQQDIKLMKmEKLVDNNTALVDKLKRFQQENEELKA 1190
Cdd:COG1196 334 eLEEELEELE-EELEEAEEELEEAEAELAEAEEALLE 369
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
999-1119 |
1.66e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 999 EKTERENRLKEFYTREYEKLRdtyiEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEI----- 1073
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALL----KEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELrqlqk 598
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1386876317 1074 KKGHEIEKKSLED---LLSEKQESLEKQINDLKSENDALNE----KLKSEEQK 1119
Cdd:PRK00409 599 GGYASVKAHELIEarkRLNKANEKKEKKKKKQKEKQEELKVgdevKYLSLGQK 651
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
976-1156 |
1.96e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 45.41 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 976 EKLEKARnelqtvyeafvQQHQAEKTERENRLKEF-----YTREYEKLRDTYIEEAEKYKMQLQEqfdnlnaaHETSKLE 1050
Cdd:pfam15558 109 EKLERAR-----------QEAEQRKQCQEQRLKEKeeelqALREQNSLQLQERLEEACHKRQLKE--------REEQKKV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1051 IEASHSEKL--ELLKKAYEaslSEIKKGHEIEKKSLEDLLSEKQESLEKQIndlKSENDALNEK-LKSEEQKRRAREKAN 1127
Cdd:pfam15558 170 QENNLSELLnhQARKVLVD---CQAKAEELLRRLSLEQSLQRSQENYEQLV---EERHRELREKaQKEEEQFQRAKWRAE 243
|
170 180
....*....|....*....|....*....
gi 1386876317 1128 LKNpqimylEQELESLKAVLEIKNEKLHQ 1156
Cdd:pfam15558 244 EKE------EERQEHKEALAELADRKIQQ 266
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
980-1191 |
2.38e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 980 KARNELQTVYEAfvQQHQAEKTERENRLKEfytreYEKLRDTYIEEAEKYKMQLQEQfdnlnaahetskleIEASHSEKL 1059
Cdd:pfam13868 32 KRIKAEEKEEER--RLDEMMEEERERALEE-----EEEKEEERKEERKRYRQELEEQ--------------IEEREQKRQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1060 EllkkAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINdLKSENDALNEKLKSEEQKRRAREK-ANLKNpqimyleq 1138
Cdd:pfam13868 91 E----EYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQ-LREEIDEFNEEQAEWKELEKEEEReEDERI-------- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1386876317 1139 eLESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKAR 1191
Cdd:pfam13868 158 -LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAK 209
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
994-1189 |
2.40e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 994 QQHQAEKTERENRLKEFYTREYEKLRDtyIEEAEKYKMQLQEQFDNLNAAHETSKLE---IEASHSEKLELLKKAYEASL 1070
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKK--AEEARIEEVMKLYEEEKKMKAEEAKKAEeakIKAEELKKAEEEKKKVEQLK 1639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1071 S----EIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSEndalnEKLKSEEQKRRAREKanlknpqimyLEQELESLKAV 1146
Cdd:PTZ00121 1640 KkeaeEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE-----EAKKAEEDEKKAAEA----------LKKEAEEAKKA 1704
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1386876317 1147 LEIKnEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQEN----EELK 1189
Cdd:PTZ00121 1705 EELK-KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDkkkaEEAK 1750
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
945-1154 |
2.59e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 945 SEREEALKQHKTLSQELVN----LRGELVTASTTCEKLEKARNELqtvyEAFVQQHQAEKTERENRLKEFyTREYEKLRD 1020
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEeaesLREDADDLEERAEELREEAAEL----ESELEEAREAVEDRREEIEEL-EEEIEELRE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1021 TY------IEEAEKYKMQLQEqfdNLNAAHETSKlEIEASHSEKLELLKKAyEASLSEIKK---GHEIEKKSLEDLLSEK 1091
Cdd:PRK02224 399 RFgdapvdLGNAEDFLEELRE---ERDELREREA-ELEATLRTARERVEEA-EALLEAGKCpecGQPVEGSPHVETIEED 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1386876317 1092 QE---SLEKQINDLKSENDALNEKLKSEEQ-----KRRAREKANLKNpqimyLEQELESLKAVLEIKNEKL 1154
Cdd:PRK02224 474 RErveELEAELEDLEEEVEEVEERLERAEDlveaeDRIERLEERRED-----LEELIAERRETIEEKRERA 539
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
941-1191 |
2.75e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 941 QHLLSEREEALKQHKTLSQEL-------VNLRGELVTASTTCEKLEKarnelqtvyEAFVQQHQAEKTERENRLKEFYTR 1013
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLdeeeaarQKLQLEKVTTEAKIKKLEE---------DILLLEDQNSKLSKERKLLEERIS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1014 EYEklrDTYIEEAEKYKMqlqeqFDNLNAAHET--SKLEIEASHSEK----LELLKKAYEASLSEIKKGHEIEKKSLEDL 1087
Cdd:pfam01576 163 EFT---SNLAEEEEKAKS-----LSKLKNKHEAmiSDLEERLKKEEKgrqeLEKAKRKLEGESTDLQEQIAELQAQIAEL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1088 ---LSEKQESLE-----------------KQINDLKSENDALNEKLKSEEQKRRAREKanlknpQIMYLEQELESLKAVL 1147
Cdd:pfam01576 235 raqLAKKEEELQaalarleeetaqknnalKKIRELEAQISELQEDLESERAARNKAEK------QRRDLGEELEALKTEL 308
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1386876317 1148 E-IKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKAR 1191
Cdd:pfam01576 309 EdTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQK 353
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
980-1127 |
2.92e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 43.00 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 980 KARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYE----KLRDtyiEEAEKYKM--QLQEQFDNLNAAHETSKLEIEA 1053
Cdd:pfam08614 20 EAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEqllaQLRE---ELAELYRSrgELAQRLVDLNEELQELEKKLRE 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386876317 1054 ShSEKLELLKkAYEASLseikkghEIEKKSLEDLLSEKQesleKQINDLKSENDALNEKLKSEEQKRRAREKAN 1127
Cdd:pfam08614 97 D-ERRLAALE-AERAQL-------EEKLKDREEELREKR----KLNQDLQDELVALQLQLNMAEEKLRKLEKEN 157
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1033-1122 |
2.97e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1033 LQE----QFDNLNAAHETSKLEIEASH----SEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESL---EKQIND 1101
Cdd:PRK05771 25 LHElgvvHIEDLKEELSNERLRKLRSLltklSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELekiEKEIKE 104
|
90 100
....*....|....*....|.
gi 1386876317 1102 LKSENDALNEKLKSEEQKRRA 1122
Cdd:PRK05771 105 LEEEISELENEIKELEQEIER 125
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
921-1197 |
3.14e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 44.17 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 921 QLKQLLACGNT---KFEALTVVIQHLLSEREEALKQHK-------TLSQELVNLRGELVTASTTCEKLEKARNELQTVYE 990
Cdd:pfam09728 5 ELMQLLNKLDSpeeKLAALCKKYAELLEEMKRLQKDLKklkkkqdQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQNK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 991 AFVQQHQAEKTERENRLKEFYTREYEKLRD--TYIEEAEKYKMQLQEQFDNLnaahetskleieashSEKLELLKKAYEa 1068
Cdd:pfam09728 85 KLKEESKKLAKEEEEKRKELSEKFQSTLKDiqDKMEEKSEKNNKLREENEEL---------------REKLKSLIEQYE- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1069 sLSEikkgheiekKSLEDLLseKQESLEKQINDLK-SENDALNEKLKSEEQKRRAREkanlKNPQIMYLEQELESLKAVL 1147
Cdd:pfam09728 149 -LRE---------LHFEKLL--KTKELEVQLAEAKlQQATEEEEKKAQEKEVAKARE----LKAQVQTLSETEKELREQL 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386876317 1148 EIKNEKLHQ-QDIkLMK-----------MEKlvdnntaLVDKLKRFQQENEELKARMDKHMA 1197
Cdd:pfam09728 213 NLYVEKFEEfQDT-LNKsnevfttfkkeMEK-------MSKKIKKLEKENLTWKRKWEKSNK 266
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1023-1166 |
3.19e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1023 IEEAEKYKMQLQEQFDNLnaahetskleIEASHSEKLELLKKAYEASlsEIKKGHEIEKKSLEDLLSEKQESLEKQINDL 1102
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNEL----------IASLEELERELEQKAEEAE--ALLKEAEKLKEELEEKKEKLQEEEDKLLEEA 571
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1386876317 1103 KSE-NDALNE-KLKSEEQKRRAREKANLKNPQIMylEQELESLKAVLEIKNEKLHQQDIKLMKMEK 1166
Cdd:PRK00409 572 EKEaQQAIKEaKKEADEIIKELRQLQKGGYASVK--AHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
900-1191 |
4.25e-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: 44.68 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 900 EKTLEltQYKTKCENQSGFILQLKQLLacgntkfEALTVVIQHLLSEREEALK------QHKTLSQELVNLRGELVTAST 973
Cdd:pfam05622 134 EATVE--TYKKKLEDLGDLRRQVKLLE-------ERNAEYMQRTLQLEEELKKanalrgQLETYKRQVQELHGKLSEESK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 974 TCEKLEKARNELQTVYEAFVQqhqaektERENRLKEfytreyeklRDTYIEEAEKYK-MQLQE----QFDNL-------- 1040
Cdd:pfam05622 205 KADKLEFEYKKLEEKLEALQK-------EKERLIIE---------RDTLRETNEELRcAQLQQaelsQADALlspssdpg 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1041 -NAAHETSKLEIEashsEKLELLKKAYEAsLSEIKKGHEIEKK-SLEDLLSEKQESLEKqindLKSENDALNEKLKSEEQ 1118
Cdd:pfam05622 269 dNLAAEIMPAEIR----EKLIRLQHENKM-LRLGQEGSYRERLtELQQLLEDANRRKNE----LETQNRLANQRILELQQ 339
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1386876317 1119 K----RRAREKANLKNPQIMYLEQELESLKavleiknEKLHQQDIKLMKMEKLVDN--NTALVDKLKRFQQENEELKAR 1191
Cdd:pfam05622 340 QveelQKALQEQGSKAEDSSLLKQKLEEHL-------EKLHEAQSELQKKKEQIEElePKQDSNLAQKIDELQEALRKK 411
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
940-1158 |
4.72e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 940 IQHLLSEREEALKQHKTLSQELVNLRGELVTASttcEKLEKARNELQTVyeafvqQHQAEKTEREnrlkefytreyeklr 1019
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELN---EEYNELQAELEAL------QAEIDKLQAE--------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1020 dtyIEEAEKYKMQLQEQFDNLNAA-----HETSKLE-IEASHS-----EKLELLKKAYEASLSEIKkgheiEKKSLEDLL 1088
Cdd:COG3883 74 ---IAEAEAEIEERREELGERARAlyrsgGSVSYLDvLLGSESfsdflDRLSALSKIADADADLLE-----ELKADKAEL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1386876317 1089 SEKQESLEKQINDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQD 1158
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAElEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
903-1124 |
4.79e-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: 44.67 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 903 LELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELvtasttcEKLEKAR 982
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL-------EKLKREI 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 983 NELQtvyeafvqqhqaekterenrlkefytREYEKLRDTyieeaekyKMQLQEQFDNLNAAHETSKLEIEASHSEKLELL 1062
Cdd:TIGR02169 402 NELK--------------------------RELDRLQEE--------LQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386876317 1063 K--KAYEASLSEIKKGHEIEKKSLEDlLSEKQESLEKQINDLKSENDALneklksEEQKRRARE 1124
Cdd:TIGR02169 448 LeiKKQEWKLEQLAADLSKYEQELYD-LKEEYDRVEKELSKLQRELAEA------EAQARASEE 504
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
900-1206 |
5.11e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 44.51 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 900 EKTLELTQ---YKTKCENQSGFILqlKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGEL--VTASTT 974
Cdd:pfam15964 350 EKTKALIQceqLKSELERQKERLE--KELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVekVTREKN 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 975 C--EKLEKARNELQT---------------VYEAFVQQHQAEKTERENRLK-----EFYTREYEKLRdtyiEEAEKYKMQ 1032
Cdd:pfam15964 428 SlvSQLEEAQKQLASqemdvtkvcgemryqLNQTKMKKDEAEKEHREYRTKtgrqlEIKDQEIEKLG----LELSESKQR 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1033 L-QEQFDNLNAAHETSKLEIEASHSEK----LELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSEND 1107
Cdd:pfam15964 504 LeQAQQDAARAREECLKLTELLGESEHqlhlTRLEKESIQQSFSNEAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQY 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1108 ALnekLKSEeqkrrarekanlkNPQIMYLEQELESLKAVLEIKNEKLHQqdiklmKMEKLVDNNTALVDKLKRFQQENEE 1187
Cdd:pfam15964 584 SL---LTSQ-------------NTFIAKLKEECCTLAKKLEEITQKSRS------EVEQLSQEKEYLQDRLEKLQKRNEE 641
|
330
....*....|....*....
gi 1386876317 1188 LKARMDKHMAISSFPRSRL 1206
Cdd:pfam15964 642 LEEQCVQHGRMHERMKQRL 660
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1019-1200 |
5.22e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1019 RDTYIEEAEKYKMQLQEQFDNLNAAHEtsklEIEASHSEKLELLKKAyEASLSEIKKGHEIEKKSLEDLlSEKQESLEKQ 1098
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALA----ELRKELEELEEELEQL-RKELEELSRQISALRKDLARL-EAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1099 INDLKSENDALNEKLKSEEQKRrarEKANlknPQIMYLEQELESLKAV--------------LEIKNEKLHQQDIKLMKM 1164
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERL---EEAE---EELAEAEAEIEELEAQieqlkeelkalreaLDELRAELTLLNEEAANL 822
|
170 180 190
....*....|....*....|....*....|....*.
gi 1386876317 1165 EKLVDNNTALVDKLKRFQQENEELKARMDKHMAISS 1200
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
944-1193 |
5.33e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 944 LSEREEALKQhKTLSQELV-----NLRGElvtASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKL 1018
Cdd:PRK04778 34 LEERKQELEN-LPVNDELEkvkklNLTGQ---SEEKFEEWRQKWDEIVTNSLPDIEEQLFEAEELNDKFRFRKAKHEINE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1019 RDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAshseklelLKKAYEaslsEIKKghEIEKKSleDLLSEKQESLEKQ 1098
Cdd:PRK04778 110 IESLLDLIEEDIEQILEELQELLESEEKNREEVEQ--------LKDLYR----ELRK--SLLANR--FSFGPALDELEKQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1099 INDLKSE---NDALNEK---LKSEEQKRRAREK-ANLKN-----PQIMY-----LEQELESLKAVL-EIKNEKLHQQDIK 1160
Cdd:PRK04778 174 LENLEEEfsqFVELTESgdyVEAREILDQLEEElAALEQimeeiPELLKelqteLPDQLQELKAGYrELVEEGYHLDHLD 253
|
250 260 270
....*....|....*....|....*....|....*....
gi 1386876317 1161 LMKM-----EKLVDNNTALVD-KLKRFQQENEELKARMD 1193
Cdd:PRK04778 254 IEKEiqdlkEQIDENLALLEElDLDEAEEKNEEIQERID 292
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1023-1194 |
5.94e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1023 IEEAEKYKMQLQEQFDNLNAahETSKLEIEASHSEKLELLKKAYEASLSEIKkgHEI-EKKSLEDLLSEKQESLEKQIND 1101
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKR--RIERLEKFIKRTENIEELIKEKEKELEEVL--REInEISSELPELREELEKLEKEVKE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1102 L---KSENDALNEKLKSEEQKRRAREkANLKN--PQIMYLEQELESL----KAVLEIK---------NEKLHQQDIKLMK 1163
Cdd:PRK03918 233 LeelKEEIEELEKELESLEGSKRKLE-EKIREleERIEELKKEIEELeekvKELKELKekaeeyiklSEFYEEYLDELRE 311
|
170 180 190
....*....|....*....|....*....|.
gi 1386876317 1164 MEKLVDNNTALVDKLKRFQQENEELKARMDK 1194
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEE 342
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1032-1188 |
6.65e-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: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1032 QLQEQFDNLNAAHETSKLEIEaSHSEKLELLKKAYEASLS---EIKKGHEIEK--KSLEDLLSEKQESLEKQI--NDLKS 1104
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELE-HKRARIELEKKASALKRQldrESDRNQELQKriRLLEKREAEAEEALREQAelNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1105 EN-DALNEKLKSEEQKR-RARE-KANLKNP------QIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALV 1175
Cdd:pfam05557 83 KYlEALNKKLNEKESQLaDAREvISCLKNElselrrQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQ 162
|
170
....*....|...
gi 1386876317 1176 DKLKRFQQENEEL 1188
Cdd:pfam05557 163 SSLAEAEQRIKEL 175
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1048-1166 |
7.77e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1048 KLEIEASHSEKLELlkkayEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSE----EQKRRAR 1123
Cdd:COG0542 403 RMEIDSKPEELDEL-----ERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEkeliEEIQELK 477
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876317 1124 EKANLKNPQIMYLEQELESLKAVLEIKNEKLHQ----QDI---------------------KLMKMEK 1166
Cdd:COG0542 478 EELEQRYGKIPELEKELAELEEELAELAPLLREevteEDIaevvsrwtgipvgkllegereKLLNLEE 545
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
976-1230 |
8.38e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 976 EKLEKARNELQTV----YEAFVQQHQAEKTERE-----NRL--------KEFYTREYEKLRDTyIEEAEKYKMQLQEQFD 1038
Cdd:PRK04863 840 RQLNRRRVELERAladhESQEQQQRSQLEQAKEglsalNRLlprlnllaDETLADRVEEIREQ-LDEAEEAKRFVQQHGN 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1039 NLnaahetSKLEIEA----SHSEKLELLKKAY---EASLSEIKKGheieKKSLEDLLSEKQE-SLEKQINDLkSENDALN 1110
Cdd:PRK04863 919 AL------AQLEPIVsvlqSDPEQFEQLKQDYqqaQQTQRDAKQQ----AFALTEVVQRRAHfSYEDAAEML-AKNSDLN 987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1111 EKLK-----SEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEklhqqdiklmkmeklvdnntalvdKLKRFQQEN 1185
Cdd:PRK04863 988 EKLRqrleqAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQ------------------------MLQELKQEL 1043
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1386876317 1186 EELKARMDKHMAI-SSFPRSRLFCKSRWRRSRKStsdSLWKTRSFC 1230
Cdd:PRK04863 1044 QDLGVPADSGAEErARARRDELHARLSANRSRRN---QLEKQLTFC 1086
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
940-1145 |
9.81e-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: 41.97 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 940 IQHLLSEREEALKQhktLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAfvQQHQAEKteRENRLKEFYTREYEKLR 1019
Cdd:pfam04012 13 IHEGLDKAEDPEKM---LEQAIRDMQSELVKARQALAQTIARQKQLERRLEQ--QTEQAKK--LEEKAQAALTKGNEELA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1020 DTYIEEAEKYKMQ---LQEQFDNLNAAHETSKLEIEASHS--EKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQES 1094
Cdd:pfam04012 86 REALAEKKSLEKQaeaLETQLAQQRSAVEQLRKQLAALETkiQQLKAKKNLLKARLKAAKAQEAVQTSLGSLSTSSATDS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1386876317 1095 LEK---QINDLKSENDALNE--KLKSEEQKRRArEKANLKNPqimylEQELESLKA 1145
Cdd:pfam04012 166 FERieeKIEEREARADAAAElaSAVDLDAKLEQ-AGIQMEVS-----EDVLARLKA 215
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
904-1187 |
1.05e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 904 ELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHllsereeALKQHKTLSQELVNLRGELVTASTTCEKLEKARN 983
Cdd:PRK01156 191 KLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNN-------AMDDYNNLKSALNELSSLEDMKNRYESEIKTAES 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 984 ELQTVYEAFVQQhqAEKTERENRL---KEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKleieashseKLE 1060
Cdd:PRK01156 264 DLSMELEKNNYY--KELEERHMKIindPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIK---------KLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1061 LLKKAYEAslseikkgHEIEKKSLEDLlsekqeslEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQI-MYLEQE 1139
Cdd:PRK01156 333 VLQKDYND--------YIKKKSRYDDL--------NNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMsAFISEI 396
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1386876317 1140 LESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEE 1187
Cdd:PRK01156 397 LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSR 444
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
976-1156 |
1.10e-03 |
|
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: 42.60 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 976 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYE-KLRDTYIEEAEKYKMQLQEqfdnLNAAHETSKLEIEAS 1054
Cdd:pfam13868 176 EEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQErKERQKEREEAEKKARQRQE----LQQAREEQIELKERR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1055 HSEKLELLKKAYEASLSEIKKGHEIEKKSLED---LLSEKQESLEKQINdlksendalneklksEEQKRRAREKANLKNP 1131
Cdd:pfam13868 252 LAEEAEREEEEFERMLRKQAEDEEIEQEEAEKrrmKRLEHRRELEKQIE---------------EREEQRAAEREEELEE 316
|
170 180
....*....|....*....|....*
gi 1386876317 1132 QIMYLEQELESLKAVLEIKNEKLHQ 1156
Cdd:pfam13868 317 GERLREEEAERRERIEEERQKKLKE 341
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
944-1156 |
1.18e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 41.66 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 944 LSEREEALKQHKTLSQELVNLRGELvtasttceklekarNELQTVYEAFVQQHQAEKTERENRLKEFyTREYEKLRDTYI 1023
Cdd:cd00176 32 LESVEALLKKHEALEAELAAHEERV--------------EALNELGEQLIEEGHPDAEEIQERLEEL-NQRWEELRELAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1024 EEAEKYK--MQLQEQFDNLnaahetskLEIEASHSEKlellkkayEASLSEIKKGHEIEkkSLEDLLsEKQESLEKQIND 1101
Cdd:cd00176 97 ERRQRLEeaLDLQQFFRDA--------DDLEQWLEEK--------EAALASEDLGKDLE--SVEELL-KKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1386876317 1102 LKSENDALNEKLKSEEQKRRAREKANLKNPQIMyLEQELESLKAVLEIKNEKLHQ 1156
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEE-LNERWEELLELAEERQKKLEE 211
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
913-1193 |
1.30e-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: 43.02 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 913 ENQSGF--ILQLKQLLACGNTKFEALTVVIQHLlseREEALKQHKTLSQELVNLRGELVTA-STTCEKLE--KARNELQT 987
Cdd:COG5185 233 EALKGFqdPESELEDLAQTSDKLEKLVEQNTDL---RLEKLGENAESSKRLNENANNLIKQfENTKEKIAeyTKSIDIKK 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 988 VYEAFVQQHQA--EKTERENRLKEFYT------REYEKLRDTYIEEAEKYKM------------QLQEQFDNLNAAHETS 1047
Cdd:COG5185 310 ATESLEEQLAAaeAEQELEESKRETETgiqnltAEIEQGQESLTENLEAIKEeienivgevelsKSSEELDSFKDTIEST 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1048 KLEIEASH---SEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQES------LEKQINDLKSENDALNEKLKSEEQ 1118
Cdd:COG5185 390 KESLDEIPqnqRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVskllneLISELNKVMREADEESQSRLEEAY 469
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876317 1119 K---RRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQdikLMKMEKLVDNNTALVDKLKRFQQENEELKARMD 1193
Cdd:COG5185 470 DeinRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQ---LEGVRSKLDQVAESLKDFMRARGYAHILALENL 544
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
921-1065 |
1.46e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 921 QLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTC------EKLEKARNELQTVYEAfVQ 994
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeeeleEELEELEEELEELEEE-LE 449
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386876317 995 QHQAEKTERENRLKEFYT-REYEKLRDTYIEEAEKYKmQLQEQFDNLNAAHETSKLEIEASHSEKL-ELLKKA 1065
Cdd:COG4717 450 ELREELAELEAELEQLEEdGELAELLQELEELKAELR-ELAEEWAALKLALELLEEAREEYREERLpPVLERA 521
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1084-1225 |
1.56e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1084 LEDLLSEKQESLEKQINDLKSENDALNEKLK-SEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLM 1162
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEqAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386876317 1163 KMEklvDNNTALVDKLKRFQQENEELKARMDKHMAISSFPRSRLFCKSRWRRSRKSTSDSLWK 1225
Cdd:COG4372 105 SLQ---EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1062-1184 |
1.57e-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: 41.43 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1062 LKKAYEASLSEIKKGH-EIEKKSLEDL---------LSEKQESLEKQINDLKSENDALNEKLKsEEQKRRAREKANLKNp 1131
Cdd:pfam13851 2 LMKNHEKAFNEIKNYYnDITRNNLELIkslkeeiaeLKKKEERNEKLMSEIQQENKRLTEPLQ-KAQEEVEELRKQLEN- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1386876317 1132 qimYLE--QELESLKAVLEIKNEKL----HQQDIKLMKMEKLVDNNTALVDKLKRFQQE 1184
Cdd:pfam13851 80 ---YEKdkQSLKNLKARLKVLEKELkdlkWEHEVLEQRFEKVERERDELYDKFEAAIQD 135
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
977-1206 |
1.62e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.14 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 977 KLEKARNELQTVYEAFVQQHQAEKTERENR---LKEFYTREYEKLRDTYIEEaeKYKMQLQEQFDNLNAAHETSKLEIEA 1053
Cdd:COG5022 814 SYLACIIKLQKTIKREKKLRETEEVEFSLKaevLIQKFGRSLKAKKRFSLLK--KETIYLQSAQRVELAERQLQELKIDV 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1054 SHSEKLELLKKAYEASLSEIKKghEIEKKSLEDL--LSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLK-- 1129
Cdd:COG5022 892 KSISSLKLVNLELESEIIELKK--SLSSDLIENLefKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKet 969
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1386876317 1130 NPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISSFPRSRL 1206
Cdd:COG5022 970 SEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILK 1046
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
955-1197 |
1.73e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.90 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 955 KTLSQELVNLRGELVtasttcEKLEKARNELQTvyEAFVQQHqaEKTERENRLKEFYTREYEKLRDTYIEEaekYKMQLQ 1034
Cdd:PTZ00440 896 KQLVEHLLNNKIDLK------NKLEQHMKIINT--DNIIQKN--EKLNLLNNLNKEKEKIEKQLSDTKINN---LKMQIE 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1035 EQFDnlnaAHETSKLEIEA---SHSEKLELLKKAYEASLSEIKK---GHEIEKKSLEDLLSE-KQESLEKQINDLKSEND 1107
Cdd:PTZ00440 963 KTLE----YYDKSKENINGndgTHLEKLDKEKDEWEHFKSEIDKlnvNYNILNKKIDDLIKKqHDDIIELIDKLIKEKGK 1038
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1108 ALNEKLKSeeqkrrarekanlknpQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEE 1187
Cdd:PTZ00440 1039 EIEEKVDQ----------------YISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIE 1102
|
250
....*....|
gi 1386876317 1188 LKARMDKHMA 1197
Cdd:PTZ00440 1103 IKNKSHEHVV 1112
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
978-1188 |
1.90e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 41.20 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 978 LEKARNELQTV-YEAFVQQHQAEKTERENRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLnaahetsKLEIEASHS 1056
Cdd:pfam05010 10 LEKARNEIEEKeLEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKV-------LEEKDQALA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1057 EKLELlkkayEASLSEIKKGHEIEKKSLEDlLSEKQESLEKQINDLKsendalnEKLKSEEQ-----KRRAREKANLKNP 1131
Cdd:pfam05010 83 DLNSV-----EKSFSDLFKRYEKQKEVISG-YKKNEESLKKCAQDYL-------ARIKKEEQryqalKAHAEEKLDQANE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1386876317 1132 QIMYLEQELESLKAVLEIkneKLHQQDIKLMKMEKLVDNNTalvdklkrfqQENEEL 1188
Cdd:pfam05010 150 EIAQVRSKAKAETAALQA---SLRKEQMKVQSLERQLEQKT----------KENEEL 193
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
931-1126 |
2.01e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 931 TKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeAFVQQHQAEKTERENRLKEF 1010
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ----AEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1011 YTREYEKLRD-TYIE---EAEKYKmQLQEQFDNLNAAHETSKLEIEASHSEKLELlkKAYEASLSEIKKGHEIEKKSLED 1086
Cdd:COG3883 92 ARALYRSGGSvSYLDvllGSESFS-DFLDRLSALSKIADADADLLEELKADKAEL--EAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1386876317 1087 LLSE---KQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA 1126
Cdd:COG3883 169 AKAEleaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
1058-1166 |
2.15e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 39.47 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1058 KLELLKKAYEASLSEIKKgheiekksLEDLLSEKQESLEKQINDLKSENDALNEKLK-SEEQKRRAREKANLKNPQIMYL 1136
Cdd:pfam13863 7 EMFLVQLALDAKREEIER--------LEELLKQREEELEKKEQELKEDLIKFDKFLKeNDAKRRRALKKAEEETKLKKEK 78
|
90 100 110
....*....|....*....|....*....|
gi 1386876317 1137 EQELESLKAVLEIKNEKLHQQDIKLMKMEK 1166
Cdd:pfam13863 79 EKEIKKLTAQIEELKSEISKLEEKLEEYKP 108
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
976-1158 |
2.79e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 40.75 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 976 EKLEKARNELQTVYE---AFVQQHQAEKTErenrlkefyTREYEKLrdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIE 1052
Cdd:pfam12795 9 KLDEAAKKKLLQDLQqalSLLDKIDASKQR---------AAAYQKA----LDDAPAELRELRQELAALQAKAEAAPKEIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1053 ASHS-EKLELLKKAYEASLSEIKKgheiEKKSLEDLLSEKQESLE---KQINDLKSENDALNEKLK---------SEEQK 1119
Cdd:pfam12795 76 ASLSlEELEQRLLQTSAQLQELQN----QLAQLNSQLIELQTRPEraqQQLSEARQRLQQIRNRLNgpappgeplSEAQR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1386876317 1120 RRAREKANLKNPQIMYLEQELES-------LKAVLEIKNEKLHQQD 1158
Cdd:pfam12795 152 WALQAELAALKAQIDMLEQELLSnnnrqdlLKARRDLLTLRIQRLE 197
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
976-1190 |
2.81e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 976 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEKYKmQLQEQFDNLNAAHETSKLEIEASH 1055
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK-AEEAKKAD-EAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1056 SEklELLKKAYEASLS-EIKKGHEIEKKSLEDLlsEKQESLEKQINDL-KSENDALNEKLKSEEQKRRARE--KA-NLKN 1130
Cdd:PTZ00121 1472 AD--EAKKKAEEAKKAdEAKKKAEEAKKKADEA--KKAAEAKKKADEAkKAEEAKKADEAKKAEEAKKADEakKAeEKKK 1547
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386876317 1131 PQIMYLEQELESLKAVLEIKNEKLHQQD--IKLMKMEKLVDNNTALVDKLKRFQQENEELKA 1190
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDknMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
978-1187 |
2.87e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.35 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 978 LEKARNELQTVyeafVQQHQAEKTERENRLKEFYTR---EYEKLRdtyieeaekykmqlqeqfdnlNAAHETSKLEIEAS 1054
Cdd:TIGR01612 673 IDALYNELSSI----VKENAIDNTEDKAKLDDLKSKidkEYDKIQ---------------------NMETATVELHLSNI 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1055 HSEKLELLkkayeASLSEIKKG--HEIEK---KSLEDLLSeKQESLEKQINDLKSENDALNE-KLKSEEQKRRAREKANL 1128
Cdd:TIGR01612 728 ENKKNELL-----DIIVEIKKHihGEINKdlnKILEDFKN-KEKELSNKINDYAKEKDELNKyKSKISEIKNHYNDQINI 801
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386876317 1129 KNPQIMYLEQELESLK---AVLEIKNEKLHQ--QDIKLMKMEKLvdnntALVDKLKRFQQENEE 1187
Cdd:TIGR01612 802 DNIKDEDAKQNYDKSKeyiKTISIKEDEIFKiiNEMKFMKDDFL-----NKVDKFINFENNCKE 860
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
994-1139 |
2.97e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.86 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 994 QQHQAEKTERENRLKEFYTREYEK------LRDTYIE------EAEKYKMQLQEQfdnlnAAHETSKLEIEASHSEKLEL 1061
Cdd:pfam15709 361 RRLQQEQLERAEKMREELELEQQRrfeeirLRKQRLEeerqrqEEEERKQRLQLQ-----AAQERARQQQEEFRRKLQEL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1062 LKKAYEASLsEIKKGHEIEKKSLEDLLSEKQ---------ESLEKQINDLKSENDAlneKLKSEEQKRRAREKANLKNPQ 1132
Cdd:pfam15709 436 QRKKQQEEA-ERAEAEKQRQKELEMQLAEEQkrlmemaeeERLEYQRQKQEAEEKA---RLEAEERRQKEEEAARLALEE 511
|
....*..
gi 1386876317 1133 IMYLEQE 1139
Cdd:pfam15709 512 AMKQAQE 518
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1001-1195 |
3.22e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1001 TERENRLKEFYT------REYEKLRDTYIEEAEKYKmqlqEQFDNLNAahETSKLeieashSEKLELLKKAYEASLSEIK 1074
Cdd:COG1340 7 SSSLEELEEKIEelreeiEELKEKRDELNEELKELA----EKRDELNA--QVKEL------REEAQELREKRDELNEKVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1075 kgheiEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRarekanlknpQIMYLEQELESlkAVLEIKNEKl 1154
Cdd:COG1340 75 -----ELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRK----------EIERLEWRQQT--EVLSPEEEK- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1386876317 1155 hqqdiklmkmeklvdnntALVDKLKRFQQENEELKARMDKH 1195
Cdd:COG1340 137 ------------------ELVEKIKELEKELEKAKKALEKN 159
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
1080-1203 |
3.26e-03 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 39.22 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1080 EKKSLEDL--LSEKQESLEKQINDLKSENDALNEKLKSE--------EQKRRAREKANLKNpQIMYLEQELESLKAVLEI 1149
Cdd:TIGR02473 15 EEQAKLELakAQAEFERLETQLQQLIKYREEYEQQALEKvgagtsalELSNYQRFIRQLDQ-RIQQQQQELALLQQEVEA 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1386876317 1150 KNEKLHQQDIKLMKMEKLVDNntalvdKLKRFQQENEELKARMDKHMAISSFPR 1203
Cdd:TIGR02473 94 KRERLLEARRELKALEKLKEK------KQKEYRAEEAKREQKEMDELATQRFRR 141
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
944-1191 |
3.38e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 944 LSEREEALKQHKTLSQELVNLRGEL-VTASTTCEKLEKARNELQTVYEAF-VQQ------HQA----EKTERENRLKEFy 1011
Cdd:PRK04863 357 LEELEERLEEQNEVVEEADEQQEENeARAEAAEEEVDELKSQLADYQQALdVQQtraiqyQQAvqalERAKQLCGLPDL- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1012 trEYEKLRDtYIEEaekYKMQLQEQFDNLNAAHEtsKLEIEASHSEKLEllkKAYEASLS-----EIKKGHEIEKKSLED 1086
Cdd:PRK04863 436 --TADNAED-WLEE---FQAKEQEATEELLSLEQ--KLSVAQAAHSQFE---QAYQLVRKiagevSRSEAWDVARELLRR 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1087 LlsEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQdiklmkMEK 1166
Cdd:PRK04863 505 L--REQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES------VSE 576
|
250 260
....*....|....*....|....*
gi 1386876317 1167 LVDNNTALVDKLKRFQQENEELKAR 1191
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLAAR 601
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
940-1230 |
3.68e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 940 IQHLLSEREEALKQHKT----LSQELVNLRG-----ELVTASTTCEKLEKARNELQTVYEA--FVQQHQaektereNRLk 1008
Cdd:COG3096 848 LERELAQHRAQEQQLRQqldqLKEQLQLLNKllpqaNLLADETLADRLEELREELDAAQEAqaFIQQHG-------KAL- 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1009 efytREYEKLRDTyieeaekykmqLQ---EQFDNLNAAHETSKleieashsEKLELLKKAYEAsLSEIKKgheiekkSLE 1085
Cdd:COG3096 920 ----AQLEPLVAV-----------LQsdpEQFEQLQADYLQAK--------EQQRRLKQQIFA-LSEVVQ-------RRP 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1086 DLLSEKQESLEKQINDLkseNDALNEKLKSEEQKR-RAREKANLKNPQIMYLEQELESLKAVLEIKNeklhqqdiklmkm 1164
Cdd:COG3096 969 HFSYEDAVGLLGENSDL---NEKLRARLEQAEEARrEAREQLRQAQAQYSQYNQVLASLKSSRDAKQ------------- 1032
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1386876317 1165 eklvdnntalvDKLKRFQQENEELKARMDKHMAISS-FPRSRLFCKSRWRRSRKStsdSLWKTRSFC 1230
Cdd:COG3096 1033 -----------QTLQELEQELEELGVQADAEAEERArIRRDELHEELSQNRSRRS---QLEKQLTRC 1085
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
936-1194 |
3.87e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.65 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 936 LTVVIQHLLSEREEalkqhkTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTEREnRLKEFYTREY 1015
Cdd:pfam05557 273 LNLRSPEDLSRRIE------QLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLK-RHKALVRRLQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1016 EKLRdTYIEEAEKYKmQLQEQFDNLNAAHETSKLEIEasHSEKLELLKKAYEASLSEIKkgHEIEKkSLEDLLSEKQ--E 1093
Cdd:pfam05557 346 RRVL-LLTKERDGYR-AILESYDKELTMSNYSPQLLE--RIEEAEDMTQKMQAHNEEME--AQLSV-AEEELGGYKQqaQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1094 SLEKQINDLKSENDaLNEKLKSEEQKRRARekanLKNPQIMYLEQELESLKAVLEIKNEKLHQQ---DIKLMKMEKLVDN 1170
Cdd:pfam05557 419 TLERELQALRQQES-LADPSYSKEEVDSLR----RKLETLELERQRLREQKNELEMELERRCLQgdyDPKKTKVLHLSMN 493
|
250 260
....*....|....*....|....*....
gi 1386876317 1171 NTALV-----DKLKRFQQENEELKARMDK 1194
Cdd:pfam05557 494 PAAEAyqqrkNQLEKLQAEIERLKRLLKK 522
|
|
| Ctf13_LRR_LRR-insertion |
cd19611 |
leucine-rich-repeat (LRR) domain and LRR insertion domain of centromere DNA-binding protein ... |
1069-1156 |
3.90e-03 |
|
leucine-rich-repeat (LRR) domain and LRR insertion domain of centromere DNA-binding protein complex CBF3 subunit C (Ctf13); Ctf13, is an F-box protein of the leucine-rich-repeat superfamily; it is a component of CEN binding factor 3 (CBF3), a complex that recognizes point centromeres found in budding yeast, associating specifically with the third centromere DNA element (CDEIII) DNA. CBF3 is comprised of two homodimers of Cep3 and Ndc10, and a Ctf13-Skp1 heterodimer. The Skp1-Ctf13 heterodimer interacts with Cep3, Ndc10 and CDEIII at a completely conserved G, centrally positioned between the TGC/CCG sites. The eight leucine-rich repeat (LRR) motifs of Ctf13 (LRR 1-8) form a solenoid structure. At the N-terminus of the Ctf13 LRR is an expanded F-box, and at the C-terminal end, an alpha-beta domain formed by insertions within the latter LRRs of Ctf13 (LRR insertion domain). This domain model includes the LLR domain and the LRR insertion domain.
Pssm-ID: 381623 Cd Length: 290 Bit Score: 40.78 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1069 SLSEIKK-GHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLK--A 1145
Cdd:cd19611 14 NPNMVKKiLKVLEKKELLDLVSEVFFGQDEEESDEEDEDDSSKNDRKKLTDDDVKEKSYKLNDPSIIRIISSLESMKnlR 93
|
90
....*....|.
gi 1386876317 1146 VLEIKNEKLHQ 1156
Cdd:cd19611 94 KLSVRGDNLYE 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
976-1197 |
4.07e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 976 EKLEKARnELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASH 1055
Cdd:PTZ00121 1293 DEAKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKK-AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1056 SEKLELLKKAYEAS--LSEIKKGHEIEKKSLED-----------LLSEKQESLEKQINDLKSENDA---LNEKLKSEEQK 1119
Cdd:PTZ00121 1371 KKKEEAKKKADAAKkkAEEKKKADEAKKKAEEDkkkadelkkaaAAKKKADEAKKKAEEKKKADEAkkkAEEAKKADEAK 1450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1120 RRAREKANLKNpqimyLEQELESLKAVLEIKneKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQEN---EELKARMDKHM 1196
Cdd:PTZ00121 1451 KKAEEAKKAEE-----AKKKAEEAKKADEAK--KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKkkaDEAKKAEEAKK 1523
|
.
gi 1386876317 1197 A 1197
Cdd:PTZ00121 1524 A 1524
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1057-1171 |
4.28e-03 |
|
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: 40.77 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1057 EKLELLKKAYEaslsEIKKgHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQkrRAREKANLKNPQIMY- 1135
Cdd:smart00787 151 ENLEGLKEDYK----LLMK-ELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELD--RAKEKLKKLLQEIMIk 223
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1386876317 1136 ------LEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNN 1171
Cdd:smart00787 224 vkkleeLEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQC 265
|
|
| PRK14160 |
PRK14160 |
heat shock protein GrpE; Provisional |
1080-1194 |
4.29e-03 |
|
heat shock protein GrpE; Provisional
Pssm-ID: 237629 [Multi-domain] Cd Length: 211 Bit Score: 40.12 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1080 EKKSLEDLLSEKQESLEKQiNDLKSENDALNEKLKSEEQKrrAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQdi 1159
Cdd:PRK14160 2 EKECKDAKHENMEEDCCKE-NENKEEDKGKEEDLEFEEIE--KEEIIEDSEESNEVKIEELKDENNKLKEENKKLENE-- 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1386876317 1160 klmkMEklvdnntALVDKLKRFQQENEELKARMDK 1194
Cdd:PRK14160 77 ----LE-------ALKDRLLRTVAEYDNYRKRTAK 100
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
900-1125 |
4.50e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 900 EKTLELTQYKTkcENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLE 979
Cdd:TIGR02168 837 ERRLEDLEEQI--EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 980 KARNELQTvyeafvQQHQAEktERENRLkefytreyeklrdtyieeaekyKMQLQEQFDNLNAAHETSkLEIEASHSEKL 1059
Cdd:TIGR02168 915 RELEELRE------KLAQLE--LRLEGL----------------------EVRIDNLQERLSEEYSLT-LEEAEALENKI 963
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1386876317 1060 ELLKKAYEASLSEIKKghEIEK------KSLEDL--LSEKQESLEKQINDLkseNDALnEKLKS--EEQKRRAREK 1125
Cdd:TIGR02168 964 EDDEEEARRRLKRLEN--KIKElgpvnlAAIEEYeeLKERYDFLTAQKEDL---TEAK-ETLEEaiEEIDREARER 1033
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1078-1188 |
5.05e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1078 EIEKKSLEDLLSEKQEsLEKQINDLKSENDALNEKLKSEEQKRRA---------------REKANLKNPQIMYLEQELES 1142
Cdd:COG1340 4 DELSSSLEELEEKIEE-LREEIEELKEKRDELNEELKELAEKRDElnaqvkelreeaqelREKRDELNEKVKELKEERDE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1386876317 1143 LKAVLEIKNEKLHQQDIKLMKMEKlvdnNTALVDKLKR------FQQENEEL 1188
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNK----AGGSIDKLRKeierleWRQQTEVL 130
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
951-1198 |
5.40e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.36 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 951 LKQHKTLSQELVNLRGELVTasttcEKLEKARNELQTVYEafvqQHQAEKTERENRLKEfYTREYEKLRD---TYIEEAE 1027
Cdd:PTZ00440 690 IKNLKKELQNLLSLKENIIK-----KQLNNIEQDISNSLN----QYTIKYNDLKSSIEE-YKEEEEKLEVykhQIINRKN 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1028 KYKMQLQEQFDNLNAAHETSK---------LEIEASHSEKLELLKKAYEASLSEIKKgHEIEKKSLEDLLSEKQESLEKQ 1098
Cdd:PTZ00440 760 EFILHLYENDKDLPDGKNTYEeflqykdtiLNKENKISNDINILKENKKNNQDLLNS-YNILIQKLEAHTEKNDEELKQL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1099 INDLKSENDALNEKlKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKlhqqdiklmkmeklvDNNTALVDKL 1178
Cdd:PTZ00440 839 LQKFPTEDENLNLK-ELEKEFNENNQIVDNIIKDIENMNKNINIIKTLNIAINRS---------------NSNKQLVEHL 902
|
250 260
....*....|....*....|
gi 1386876317 1179 KRFQQeneELKARMDKHMAI 1198
Cdd:PTZ00440 903 LNNKI---DLKNKLEQHMKI 919
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
990-1190 |
6.48e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 990 EAFVQQHQAEKT---ERENRLKEFYtREYEKLRDTYIEEAEKYKM--QLQEQFDNLNAAHET-SKLEIEASH------SE 1057
Cdd:COG4913 210 DDFVREYMLEEPdtfEAADALVEHF-DDLERAHEALEDAREQIELlePIRELAERYAAARERlAELEYLRAAlrlwfaQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1058 KLELLKKAYEASLSEIKKgHEIEKKSLEDLLSEKQESLE-----------KQINDLKSENDALNEKLKSEEQKRRAREKA 1126
Cdd:COG4913 289 RLELLEAELEELRAELAR-LEAELERLEARLDALREELDeleaqirgnggDRLEQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876317 1127 ----NLKNPQImylEQELESLKAVLEIKNEKLHQQDiklmkmEKLVDNNTALVDKLKRFQQENEELKA 1190
Cdd:COG4913 368 laalGLPLPAS---AEEFAALRAEAAALLEALEEEL------EALEEALAEAEAALRDLRRELRELEA 426
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
998-1111 |
7.41e-03 |
|
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: 38.00 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 998 AEKTERENRLKEfytreYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHEtsKLEIE----ASHSEKLELLKKAY------- 1066
Cdd:pfam07926 1 AELSSLQSEIKR-----LKEEAADAEAQLQKLQEDLEKQAEIAREAQQ--NYERElvlhAEDIKALQALREELnelkaei 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1386876317 1067 ---EASLSEIKKGHEIEKKSLEdllsEKQESLEKQINDLKSENDALNE 1111
Cdd:pfam07926 74 aelKAEAESAKAELEESEESWE----EQKKELEKELSELEKRIEDLNE 117
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
931-1192 |
7.65e-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: 40.54 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 931 TKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeafvQQHQAEKTERENRLKEF 1010
Cdd:pfam01576 636 TRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALE-------QQVEEMKTQLEELEDEL 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1011 YTREYEKLR----------------DTYIEEAEKYKMQLQEQFDNL------------NAAHETSKLE---------IEA 1053
Cdd:pfam01576 709 QATEDAKLRlevnmqalkaqferdlQARDEQGEEKRRQLVKQVRELeaelederkqraQAVAAKKKLEldlkeleaqIDA 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1054 SHSEKLELLK--KAYEASLSEIKKGHEIEKKSLEDLLSEKQESlEKQINDLKSENDALNEKLKSEEQKRR---------- 1121
Cdd:pfam01576 789 ANKGREEAVKqlKKLQAQMKDLQRELEEARASRDEILAQSKES-EKKLKNLEAELLQLQEDLAASERARRqaqqerdela 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1122 -------------AREKANLKNpQIMYLEQELESLKAVLEIKNEKLH--QQDIKLMKMEKLVDNNTALVDKLKRFQQE-- 1184
Cdd:pfam01576 868 deiasgasgksalQDEKRRLEA-RIAQLEEELEEEQSNTELLNDRLRksTLQVEQLTTELAAERSTSQKSESARQQLErq 946
|
....*...
gi 1386876317 1185 NEELKARM 1192
Cdd:pfam01576 947 NKELKAKL 954
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
976-1115 |
8.36e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 40.51 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 976 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRdtyieeaEKYKMQLQEQFDNLNAAHEtSKLEiEASH 1055
Cdd:pfam09731 316 RALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIR-------ESYEEKLRTELERQAEAHE-EHLK-DVLV 386
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1386876317 1056 SEKLELlkkayeaslsEIKKGHEIEKKSLE--DLLSEKQESLEKQINDLK----SENDALNEKLKS 1115
Cdd:pfam09731 387 EQEIEL----------QREFLQDIKEKVEEerAGRLLKLNELLANLKGLEkatsSHSEVEDENRKA 442
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
940-1191 |
8.85e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 39.79 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 940 IQHLLSEREEALKQHKTLSQELVNLRGELVTA-------STTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLkefYT 1012
Cdd:pfam15905 82 IRALVQERGEQDKRLQALEEELEKVEAKLNAAvrektslSASVASLEKQLLELTRVNELLKAKFSEDGTQKKMSS---LS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1013 REYEKLRDTyIEEAEKYKMQLQEqfdnlnaahetsKLEIeashseKLELLKKAYEASLSEIKKgheiekksledlLSEKQ 1092
Cdd:pfam15905 159 MELMKLRNK-LEAKMKEVMAKQE------------GMEG------KLQVTQKNLEHSKGKVAQ------------LEEKL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1093 ESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKnpqIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKlvdnnt 1172
Cdd:pfam15905 208 VSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLD---IAQLEELLKEKNDEIESLKQSLEEKEQELSKQIK------ 278
|
250
....*....|....*....
gi 1386876317 1173 ALVDKLKRFQQENEELKAR 1191
Cdd:pfam15905 279 DLNEKCKLLESEKEELLRE 297
|
|
| Snf7 |
pfam03357 |
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ... |
1085-1193 |
9.17e-03 |
|
Snf7; This family of proteins are involved in protein sorting and transport from the endosome to the vacuole/lysosome in eukaryotic cells. Vacuoles/lysosomes play an important role in the degradation of both lipids and cellular proteins. In order to perform this degradative function, vacuoles/lysosomes contain numerous hydrolases which have been transported in the form of inactive precursors via the biosynthetic pathway and are proteolytically activated upon delivery to the vacuole/lysosome. The delivery of transmembrane proteins, such as activated cell surface receptors to the lumen of the vacuole/lysosome, either for degradation/downregulation, or in the case of hydrolases, for proper localization, requires the formation of multivesicular bodies (MVBs). These late endosomal structures are formed by invaginating and budding of the limiting membrane into the lumen of the compartment. During this process, a subset of the endosomal membrane proteins is sorted into the forming vesicles. Mature MVBs fuse with the vacuole/lysosome, thereby releasing cargo containing vesicles into its hydrolytic lumen for degradation. Endosomal proteins that are not sorted into the intralumenal MVB vesicles are either recycled back to the plasma membrane or Golgi complex, or remain in the limiting membrane of the MVB and are thereby transported to the limiting membrane of the vacuole/lysosome as a consequence of fusion. Therefore, the MVB sorting pathway plays a critical role in the decision between recycling and degradation of membrane proteins. A few archaeal sequences are also present within this family.
Pssm-ID: 460896 [Multi-domain] Cd Length: 168 Bit Score: 38.37 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1085 EDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNpQIMYLEQELESLKAVLE-IKNEKLHQQDIKLMK 1163
Cdd:pfam03357 10 IRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEK-QLDQLDGQLSNLEQQRMaIENAKSNQEVLNAMK 88
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90 100 110
....*....|....*....|....*....|....*...
gi 1386876317 1164 --------MEKLVDnntalVDKLKRFQQENEELKARMD 1193
Cdd:pfam03357 89 qgakamkaMNKLMD-----IDKIDKLMDEIEDQMEKAD 121
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| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1062-1200 |
9.99e-03 |
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reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.42 E-value: 9.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876317 1062 LKKAYEASLSEIKKGHEIEKKSLEDllSEKQESLEKQINDLksendaLNEKLKSEEQkrrarekanlkNPQIMYLEQEL- 1140
Cdd:TIGR01612 546 LKESYELAKNWKKLIHEIKKELEEE--NEDSIHLEKEIKDL------FDKYLEIDDE-----------IIYINKLKLELk 606
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386876317 1141 ESLKAVLEiKNEKLHqqdiKLMKMEKLVDNNTALVDKLKRFQ--QENEELKARMDKHMAISS 1200
Cdd:TIGR01612 607 EKIKNISD-KNEYIK----KAIDLKKIIENNNAYIDELAKISpyQVPEHLKNKDKIYSTIKS 663
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