|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
919-1215 |
3.43e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 81.26 E-value: 3.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 919 ILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTAST----TCEKLEKARNELQTVyEAFVQ 994
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisaLRKDLARLEAEVEQL-EERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 995 QHQAEKTERENRLKEfYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEkLELLKKAY---EASLS 1071
Cdd:TIGR02168 751 QLSKELTELEAEIEE-LEERLEEAEEE-LAEAEAEIEELEAQIEQLKEELKALREALDELRAE-LTLLNEEAanlRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1072 EIKKGHEIEKKSLEDL------LSEKQESLEKQINDLKSE--------NDALNEKLKSEEQKRRAREKANLKNPQIMYLE 1137
Cdd:TIGR02168 828 SLERRIAATERRLEDLeeqieeLSEDIESLAAEIEELEELieeleselEALLNERASLEEALALLRSELEELSEELRELE 907
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50348611 1138 QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNtalvdklkrFQQENEELKARMDKHMAISRQLSTEQAVLQESLEK 1215
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNL---------QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
946-1232 |
5.59e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 5.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 946 EREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFY-----------TRE 1014
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellaelarleqDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1015 YEKLRdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAShSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQES 1094
Cdd:COG1196 306 RLEER---RRELEERLEELEEELAELEEELEELEEELEEL-EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1095 LEKQINDLKSENDALNEKLKSEE----QKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 1170
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEEleeaEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50348611 1171 NTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLW 1232
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
943-1218 |
8.76e-13 |
|
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: 73.17 E-value: 8.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 943 LLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQ---------QHQAEKTERENRLKEFYTR 1013
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANeisrleqqkQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1014 EYEKL---RDTYIEEA---EKYKMQLQEQFDNLNAAHETSKLEIEASHSeKLELLKKAYEASLSEIkkgHEIEKKslEDL 1087
Cdd:TIGR02168 324 QLEELeskLDELAEELaelEEKLEELKEELESLEAELEELEAELEELES-RLEELEEQLETLRSKV---AQLELQ--IAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1088 LSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNpQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKL 1167
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA-ELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50348611 1168 VDnntALVDKLKRFQQENEELKARMDKHMAISR----------QLSTEQAVLQESLEKESK 1218
Cdd:TIGR02168 477 LD---AAERELAQLQARLDSLERLQENLEGFSEgvkallknqsGLSGILGVLSELISVDEG 534
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
940-1230 |
1.18e-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: 72.78 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 940 IQHLLSEREEALKqHKTLSQELVNLRGELVTASTtcEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEfytreyeklr 1019
Cdd:TIGR02168 202 LKSLERQAEKAER-YKELKAELRELELALLVLRL--EELREELEELQEELKEAEEELEELTAELQELEEK---------- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1020 dtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKlELLKKAYEASLSEIKKGHEI--EKKSLEDLLSEKQESLEK 1097
Cdd:TIGR02168 269 ---LEELRLEVSELEEEIEELQKELYALANEISRLEQQK-QILRERLANLERQLEELEAQleELESKLDELAEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1098 QINDLKSENDALNEKLKSEEQKRRAREKANLKnpqimyLEQELESLK-AVLEIKNE-KLHQQDIKLMKMEKlvdnnTALV 1175
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEE------LEEQLETLRsKVAQLELQiASLNNEIERLEARL-----ERLE 413
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 50348611 1176 DKLKRFQQENEELKARMDKH--MAISRQLSTEQAVLQESLEKESKVNKRLSMENEEL 1230
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAelKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
976-1230 |
3.11e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.64 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 976 EKLEKARNELQTVYE--AFVQQHQAEKTERENRLKEfytreyEKlrdtyiEEAEKYKMQLQEqfdnlnaahetsKLEIEA 1053
Cdd:TIGR02169 170 RKKEKALEELEEVEEniERLDLIIDEKRQQLERLRR------ER------EKAERYQALLKE------------KREYEG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1054 ShseklELL--KKAYEASLSEIKKGHEIEKKSLEDLLSEKQEsLEKQINDLKSENDALNEKLK--SEEQKRRAREKanlk 1129
Cdd:TIGR02169 226 Y-----ELLkeKEALERQKEAIERQLASLEEELEKLTEEISE-LEKRLEEIEQLLEELNKKIKdlGEEEQLRVKEK---- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1130 npqIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQE--------NEELKARMDKHMAISRQ 1201
Cdd:TIGR02169 296 ---IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdklTEEYAELKEELEDLRAE 372
|
250 260
....*....|....*....|....*....
gi 50348611 1202 LSTEQAVLQESLEKESKVNKRLSMENEEL 1230
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREI 401
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
994-1231 |
5.67e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 994 QQHQAEKTERENRLK----EFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAShSEKLELLKKAYEAS 1069
Cdd:COG1196 216 RELKEELKELEAELLllklRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1070 LSEIKkghEIEKKslEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpQIMYLEQELESLKAVLEI 1149
Cdd:COG1196 294 LAELA---RLEQD--IARLEERRRELEERLEELEEELAELEEELEELEEELEELEE------ELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1150 KNEKLHQQDIKLMKMEKLVDNNT----ALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSM 1225
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAeellEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
....*.
gi 50348611 1226 ENEELL 1231
Cdd:COG1196 443 ALEEAA 448
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
900-1222 |
8.70e-11 |
|
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: 66.92 E-value: 8.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 900 EKTLELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKT-LSQELVNLRGELVTAsttcEKL 978
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDeEEEEEEKSRLKKEEK----EEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 979 EKARNELQTVYEAFVQQHQAEKTERENRLKEfytREYEKLRdTYIEEAEKYKMQLQEQFDNL-NAAHETSKLEIEASHSE 1057
Cdd:pfam02463 766 KSELSLKEKELAEEREKTEKLKVEEEKEEKL---KAQEEEL-RALEEELKEEAELLEEEQLLiEQEEKIKEEELEELALE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1058 KLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQinDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLE 1137
Cdd:pfam02463 842 LKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ--KLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEI 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1138 QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKES 1217
Cdd:pfam02463 920 EERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 999
|
....*
gi 50348611 1218 KVNKR 1222
Cdd:pfam02463 1000 LEEEK 1004
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
976-1235 |
1.37e-10 |
|
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: 66.15 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 976 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDtyIEEAEKYKMQLQEQFDNLNAAHetSKLEIEASH 1055
Cdd:TIGR00618 127 ETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMN--LFPLDQYTQLALMEFAKKKSLH--GKAELLTLR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1056 SEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKqindLKSENDALNEKLKSEEQKRRAREKanlknpqimy 1135
Cdd:TIGR00618 203 SQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY----LTQKREAQEEQLKKQQLLKQLRAR---------- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1136 lEQELESLKAVLEIKNEKLHQQdiklMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEK 1215
Cdd:TIGR00618 269 -IEELRAQEAVLEETQERINRA----RKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343
|
250 260
....*....|....*....|....*..
gi 50348611 1216 ESKVNKRLSME-------NEELLWKLH 1235
Cdd:TIGR00618 344 RRLLQTLHSQEihirdahEVATSIREI 370
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
943-1230 |
1.84e-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: 65.47 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 943 LLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKE---FYTREYEKLR 1019
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkigELEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1020 DTY------IEEAEKYKMQLQEQFDNLNAAHETSKLEIE------ASHSEKLELLKKAYEASLSEIKkghEIEKKSLEdl 1087
Cdd:TIGR02169 308 RSIaekereLEDAEERLAKLEAEIDKLLAEIEELEREIEeerkrrDKLTEEYAELKEELEDLRAELE---EVDKEFAE-- 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1088 LSEKQESLEKQINDLKSENDALNEKL--KSEEQKRRAREKANLKNpQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKme 1165
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELdrLQEELQRLSEELADLNA-AIAGIEAKINELEEEKEDKALEIKKQEWKLEQ-- 459
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50348611 1166 klvdnntaLVDKLKRFQQENEELKarmdkhmaisrqlsteqavlqeslEKESKVNKRLSMENEEL 1230
Cdd:TIGR02169 460 --------LAADLSKYEQELYDLK------------------------EEYDRVEKELSKLQREL 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
916-1229 |
7.03e-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: 63.93 E-value: 7.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 916 SGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEK---ARNELQTVYEAF 992
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeeeKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 993 VQQHQAEKTERENRLKEFYTReyeklrdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSE 1072
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEAR---------IEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1073 IKKghEIEKKSLED--LLSEKQES------LEKQINDLKSENDALN---EKLKSEEQKRRA-------------REKANL 1128
Cdd:TIGR02169 817 IEQ--KLNRLTLEKeyLEKEIQELqeqridLKEQIKSIEKEIENLNgkkEELEEELEELEAalrdlesrlgdlkKERDEL 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1129 KNpQIMYLEQELESLKAVLEIKNEKLHQQDIKLmkmEKLVDNNTALVDKLKRFQQENEELkarmdkhmAISRQLSTEQAV 1208
Cdd:TIGR02169 895 EA-QLRELERKIEELEAQIEKKRKRLSELKAKL---EALEEELSEIEDPKGEDEEIPEEE--------LSLEDVQAELQR 962
|
330 340
....*....|....*....|.
gi 50348611 1209 LQESLEKESKVNKRLSMENEE 1229
Cdd:TIGR02169 963 VEEEIRALEPVNMLAIQEYEE 983
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
900-1236 |
1.76e-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: 62.35 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 900 EKTLELTQYKTKCENQSGFILQLK-QLLACGNTKFEALTVVIQHLLSEREEALKQHKT-----------LSQELVNLRGE 967
Cdd:TIGR04523 271 EKQKELEQNNKKIKELEKQLNQLKsEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNqisqnnkiisqLNEQISQLKKE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 968 LVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTEREN--------RLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDN 1039
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNlesqindlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1040 LNAAHETSKLEIEASHSE---------KLELLKKAYEASLSEIKKGHEIEKKSLEDLLSE------KQESLEKQINDLKS 1104
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQdsvkeliikNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElkskekELKKLNEEKKELEE 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1105 ENDALNEKLKSEEQKRRAREKA-NLKNPQIMYLEQELESLKAVL---EIKNEKLH-QQDIKLMKMEK--LVDNNTALVDK 1177
Cdd:TIGR04523 511 KVKDLTKKISSLKEKIEKLESEkKEKESKISDLEDELNKDDFELkkeNLEKEIDEkNKEIEELKQTQksLKKKQEEKQEL 590
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 50348611 1178 LKRFQQENEELKARMDKHMAISRQLSTEqavlqesLEKESKVNKRLSMENEELLWKLHN 1236
Cdd:TIGR04523 591 IDQKEKEKKDLIKEIEEKEKKISSLEKE-------LEKAKKENEKLSSIIKNIKSKKNK 642
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
934-1159 |
2.02e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 934 EALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQaektERENRLKEFYTR 1013
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA----EAEEELEELAEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1014 EYEKLRDtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKkgheiEKKSLEDLLSEKQE 1093
Cdd:COG1196 388 LLEALRA--AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE-----AAEEEAELEEEEEA 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50348611 1094 SLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDI 1159
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAV 526
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
948-1230 |
3.81e-09 |
|
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: 60.91 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 948 EEALKQHKTLSQELVNLRGELVTASTTC-EKLEKARNELQtvYEAFVQQHQAEKTERENRLKEFYTREYEKLRDtYIEEA 1026
Cdd:pfam05557 44 DRESDRNQELQKRIRLLEKREAEAEEALrEQAELNRLKKK--YLEALNKKLNEKESQLADAREVISCLKNELSE-LRRQI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1027 EKYKMQLQEQFDNLNAAHEtsKLEIEASHSEKLELLKKAYEASLSEIKKgHEIEKKSLEDLLsEKQESLEKQINDLKSEN 1106
Cdd:pfam05557 121 QRAELELQSTNSELEELQE--RLDLLKAKASEAEQLRQNLEKQQSSLAE-AEQRIKELEFEI-QSQEQDSEIVKNSKSEL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1107 DALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLK-------------AVLEIKNEKLHQqdiKLMKMEKLVDNNT- 1172
Cdd:pfam05557 197 ARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKrklereekyreeaATLELEKEKLEQ---ELQSWVKLAQDTGl 273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50348611 1173 ------ALVDKLKRFQQENEELKARMD------KHMAIS-RQLSTEQAVLQESLEKESKVNKRLSMENEEL 1230
Cdd:pfam05557 274 nlrspeDLSRRIEQLQQREIVLKEENSsltssaRQLEKArRELEQELAQYLKKIEDLNKKLKRHKALVRRL 344
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
979-1227 |
5.11e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.80 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 979 EKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKL-----EIEA 1053
Cdd:COG3206 148 ELAAAVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKE-LEEAEAALEEFRQKNGLVDLSEEAKLLlqqlsELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1054 SHSEkLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQ-ESLEKQINDLKSENDALNEKLKSeeqkrrarekanlKNPQ 1132
Cdd:COG3206 227 QLAE-ARAELAEAEARLAALRAQLGSGPDALPELLQSPViQQLRAQLAELEAELAELSARYTP-------------NHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1133 IMYLEQELESLKAVLEIKNEKLhQQDIKlMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQES 1212
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRI-LASLE-AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL 370
|
250
....*....|....*..
gi 50348611 1213 LEK--ESKVNKRLSMEN 1227
Cdd:COG3206 371 LQRleEARLAEALTVGN 387
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
865-1187 |
5.12e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 865 RKNLFTALNAVEKSRQKNPrsLCIQPQTAPDalppEKTLeLTQYKTKCENQSGFILQLKQLLacgnTKFEALTVVIQHLL 944
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCP--VCGRELTEEH----RKEL-LEEYTAELKRIEKELKEIEEKE----RKLRKELRELEKVL 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 945 SEREEALKQHKTLSQeLVNLRGELvtASTTCEKLEKARNELQTVYEAFVQQhQAEKTERENRLKEFytREYEKLRdtyiE 1024
Cdd:PRK03918 490 KKESELIKLKELAEQ-LKELEEKL--KKYNLEELEKKAEEYEKLKEKLIKL-KGEIKSLKKELEKL--EELKKKL----A 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1025 EAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEA--SLSEIKKGHEIEKKSLEDL---LSEKQESLEKQI 1099
Cdd:PRK03918 560 ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLeeeLDKAFEELAETE 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1100 NDLKSENDALNEKLK--SEEQKRRAREKANLKNPQIMYLEQELESLKAVLE--------IKNEK--LHQQDIKLMKMEKL 1167
Cdd:PRK03918 640 KRLEELRKELEELEKkySEEEYEELREEYLELSRELAGLRAELEELEKRREeikktlekLKEELeeREKAKKELEKLEKA 719
|
330 340
....*....|....*....|
gi 50348611 1168 VDNNTALVDKLKRFQQENEE 1187
Cdd:PRK03918 720 LERVEELREKVKKYKALLKE 739
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
939-1259 |
5.54e-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: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 939 VIQH--LLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYE---AFVQQHQAEKTERENRL----KE 1009
Cdd:pfam17380 277 IVQHqkAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDrqaAIYAEQERMAMERERELerirQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1010 FYTREYEKLRD-------TYIEEAEKYKMQLQEQFD----NLNAAHETSKLEIEasHSEKLELLKKAYEASLSEIKKGHE 1078
Cdd:pfam17380 357 ERKRELERIRQeeiameiSRMRELERLQMERQQKNErvrqELEAARKVKILEEE--RQRKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1079 IEKKSLED-----LLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLK-AVLEIKNE 1152
Cdd:pfam17380 435 REVRRLEEerareMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKqAMIEEERK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1153 KlhqqdiKLMKMEkLVDNNTALVDKLKRFQQENEELKAR-MDKHMAISRQL--STEQAVLQESLEKESKVNKRLsMENEE 1229
Cdd:pfam17380 515 R------KLLEKE-MEERQKAIYEEERRREAEEERRKQQeMEERRRIQEQMrkATEERSRLEAMEREREMMRQI-VESEK 586
|
330 340 350
....*....|....*....|....*....|
gi 50348611 1230 LLWKLhngdlcsPKRSPTSSAIPLQSPRNS 1259
Cdd:pfam17380 587 ARAEY-------EATTPITTIKPIYRPRIS 609
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
931-1236 |
7.76e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 7.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 931 TKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELvtasttcEKLEKARNELQTVyeafvqqhQAEKTERENRLKEF 1010
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL-------EELEERHELYEEA--------KAKKEELERLKKRL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1011 YTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAahETSKLEIEASHseklelLKKAyeasLSEIKK--------GHEIEKK 1082
Cdd:PRK03918 382 TGLTPEKLEKE-LEELEKAKEEIEEEISKITA--RIGELKKEIKE------LKKA----IEELKKakgkcpvcGRELTEE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1083 SLEDLLSEKQESLEKQINDLKsENDALNEKLKSEEQKrraREKANLKNPQIMYLEQELESLKAVleikNEKLHQQDIKlm 1162
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELK-EIEEKERKLRKELRE---LEKVLKKESELIKLKELAEQLKEL----EEKLKKYNLE-- 518
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50348611 1163 kmeklvdnntalvdKLKRFQQENEELKARMDKhmaisrqLSTEQAVLQESLEKESKVNKRLsmenEELLWKLHN 1236
Cdd:PRK03918 519 --------------ELEKKAEEYEKLKEKLIK-------LKGEIKSLKKELEKLEELKKKL----AELEKKLDE 567
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
976-1229 |
9.22e-09 |
|
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: 58.78 E-value: 9.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 976 EKLEKARNELQTVYEAFVQQH----------QAEKTERENR-LKEFYTREYEKLRDTYIEEAEKyKMQLQEQFDNLNAAH 1044
Cdd:pfam13868 61 EEKEEERKEERKRYRQELEEQieereqkrqeEYEEKLQEREqMDEIVERIQEEDQAEAEEKLEK-QRQLREEIDEFNEEQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1045 ETSK-LEIEAshsEKLELLK-KAYEASLSEIKKGHEIEKKSLE---DLLSEKQESLEKQINDLKSENDALNEKLKSEEQK 1119
Cdd:pfam13868 140 AEWKeLEKEE---EREEDERiLEYLKEKAEREEEREAEREEIEeekEREIARLRAQQEKAQDEKAERDELRAKLYQEEQE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1120 RRAREKAnlknpqimyLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEElKARMDKHMAIS 1199
Cdd:pfam13868 217 RKERQKE---------REEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEE-IEQEEAEKRRM 286
|
250 260 270
....*....|....*....|....*....|
gi 50348611 1200 RQLSTEQAVLQESLEKESKvnKRLSMENEE 1229
Cdd:pfam13868 287 KRLEHRRELEKQIEEREEQ--RAAEREEEL 314
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
940-1142 |
1.23e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 940 IQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAfVQQHQAEKTERENRLKefytREYEKLR 1019
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-AEAELAEAEEALLEAE----AELAEAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1020 DTYIEEAEKYKMQLQEQFDNLNA-AHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQ 1098
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQlEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 50348611 1099 INDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELES 1142
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
938-1245 |
2.80e-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: 58.44 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 938 VVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYeafvQQHQAEKTERENRLKEFYTREYEK 1017
Cdd:pfam02463 162 AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYY----QLKEKLELEEEYLLYLDYLKLNEE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1018 LRDTYIE----EAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQE 1093
Cdd:pfam02463 238 RIDLLQEllrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1094 SLEKQINDLKSENDAL----NEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIK------LMK 1163
Cdd:pfam02463 318 ESEKEKKKAEKELKKEkeeiEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSaaklkeEEL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1164 MEKLVDNNTALvDKLKRFQQENEELKARMDKhmaisrqLSTEQAVLQESLEKESKVNKRLSmENEELLWKLHNGDLCSPK 1243
Cdd:pfam02463 398 ELKSEEEKEAQ-LLLELARQLEDLLKEEKKE-------ELEILEEEEESIELKQGKLTEEK-EELEKQELKLLKDELELK 468
|
..
gi 50348611 1244 RS 1245
Cdd:pfam02463 469 KS 470
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
940-1101 |
4.28e-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: 55.32 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 940 IQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVY---EAFVQQHQAEKTERENRL------KEF 1010
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIkrlELEIEEVEARIKKYEEQLgnvrnnKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1011 --YTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAsHSEKLELLKKAYEASLSEIKKghEIEKksledlL 1088
Cdd:COG1579 92 eaLQKEIESLKRR-ISDLEDEILELMERIEELEEELAELEAELAE-LEAELEEKKAELDEELAELEA--ELEE------L 161
|
170
....*....|...
gi 50348611 1089 SEKQESLEKQIND 1101
Cdd:COG1579 162 EAEREELAAKIPP 174
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
904-1149 |
6.05e-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: 57.37 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 904 ELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARN 983
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 984 ELQTVYEAF---VQQHQAEKTERENRLKEFyTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE 1060
Cdd:TIGR02168 863 ELEELIEELeseLEALLNERASLEEALALL-RSELEELSEE-LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1061 LLKKA---YEASLSEIKKgHEIEKKSLEDLLSEKQESLEKQINDLKSEN-DALNEklkSEEQKRRAREKANlknpQIMYL 1136
Cdd:TIGR02168 941 LQERLseeYSLTLEEAEA-LENKIEDDEEEARRRLKRLENKIKELGPVNlAAIEE---YEELKERYDFLTA----QKEDL 1012
|
250
....*....|....
gi 50348611 1137 EQELESL-KAVLEI 1149
Cdd:TIGR02168 1013 TEAKETLeEAIEEI 1026
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
940-1235 |
6.54e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 6.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 940 IQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEkterenrLKEFYTREYEKLR 1019
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKE-------LLEEYTAELKRIE 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1020 DTyIEEAEKYKMQLQEqfdnlnaahETSKLEIEASHSEKLELLKKAYEaSLSEIKKghEIEKKSLEDL--LSEKQESLEK 1097
Cdd:PRK03918 466 KE-LKEIEEKERKLRK---------ELRELEKVLKKESELIKLKELAE-QLKELEE--KLKKYNLEELekKAEEYEKLKE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1098 QINDLKSENDALNEKLKSEEQKRRAREKANLKnpqIMYLEQELESLKAVLEIKN-EKLHQQDIKLMKMEKLVDNNTALVD 1176
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEELKKKLAELEKK---LDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKD 609
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 50348611 1177 KLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLWKLH 1235
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEY 668
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
932-1215 |
8.43e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 8.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 932 KFEALTVVIQHLLSERE----EALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeafvqQHQAEKTERENRL 1007
Cdd:PRK03918 183 KFIKRTENIEELIKEKEkeleEVLREINEISSELPELREELEKLEKEVKELEELKEEIE--------ELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1008 KefytREYEKLRDT--YIEEAEKYKMQLQEQfdnlnaAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIekksle 1085
Cdd:PRK03918 255 R----KLEEKIRELeeRIEELKKEIEELEEK------VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1086 dlLSEKQESLEKQINDLKSENDALNEKLKSEEqkrrarekanlknpqimyleqELESLKAVLEIKNEKLHQQDIKLMKME 1165
Cdd:PRK03918 319 --LEEEINGIEERIKELEEKEERLEELKKKLK---------------------ELEKRLEELEERHELYEEAKAKKEELE 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 50348611 1166 KLVDNNTA-----LVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEK 1215
Cdd:PRK03918 376 RLKKRLTGltpekLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
946-1226 |
8.95e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 56.44 E-value: 8.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 946 EREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQA---EKTERENRLKEF-----------Y 1011
Cdd:pfam07888 67 DREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDAllaQRAAHEARIRELeediktltqrvL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1012 TREYEKLRDTyiEEAEKYKMQLQEQfdnlNAAHETSKLEIEASHSEKLELLKKAYEAslseikKGHEIEKKSLEDLLSEK 1091
Cdd:pfam07888 147 ERETELERMK--ERAKKAGAQRKEE----EAERKQLQAKLQQTEEELRSLSKEFQEL------RNSLAQRDTQVLQLQDT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1092 QESLEKQINDlKSENDALNEKLKseEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKME-KLVDN 1170
Cdd:pfam07888 215 ITTLTQKLTT-AHRKEAENEALL--EELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTlQLADA 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 50348611 1171 NTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSME 1226
Cdd:pfam07888 292 SLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
903-1185 |
1.15e-07 |
|
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: 56.27 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 903 LELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKA- 981
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQi 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 982 ----------RNELQTVYEAFVQQH-----QAEKTERENRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHET 1046
Cdd:pfam05483 537 enleekemnlRDELESVREEFIQKGdevkcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQE 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1047 SKLEIEASHSE------------KLEL----LKKAYEASLSEIKKGHEIEKKSLEDLLSEKQES---------LEKQInD 1101
Cdd:pfam05483 617 NKALKKKGSAEnkqlnayeikvnKLELelasAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAkaiadeavkLQKEI-D 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1102 LK-----SENDALNEKLKSEEQK---RRAREKANLKNPqimylEQELESLKAVLEIKNEKLHQQdikLMKMEKLVDNNTA 1173
Cdd:pfam05483 696 KRcqhkiAEMVALMEKHKHQYDKiieERDSELGLYKNK-----EQEQSSAKAALEIELSNIKAE---LLSLKKQLEIEKE 767
|
330
....*....|..
gi 50348611 1174 LVDKLKRFQQEN 1185
Cdd:pfam05483 768 EKEKLKMEAKEN 779
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
946-1215 |
1.34e-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: 56.34 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 946 EREEALKQHKTLSQELVNLRG-------ELVTASTTCEKLEKARNELQ-TVYEAfvQQHQAE-----KTERENRLKEfyt 1012
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAqlakkeeELQAALARLEEETAQKNNALkKIREL--EAQISElqedlESERAARNKA--- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1013 reyEKLRDTYIEEAEKYKMQLQEQFDNLNAAHE-TSKLEIEASHSEK-LELLKKAYEASLSEIKKGH-----------EI 1079
Cdd:pfam01576 291 ---EKQRRDLGEELEALKTELEDTLDTTAAQQElRSKREQEVTELKKaLEEETRSHEAQLQEMRQKHtqaleelteqlEQ 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1080 EKKSLEDLLSEKQeSLEKQINDLKSENDALNE-KLKSEEQKRRA---------------REKANLkNPQIMYLEQELESL 1143
Cdd:pfam01576 368 AKRNKANLEKAKQ-ALESENAELQAELRTLQQaKQDSEHKRKKLegqlqelqarlseseRQRAEL-AEKLSKLQSELESV 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1144 KAVL---EIKNEKLHQQ----DIKLMKMEKLVDNNT----ALVDKLKRFQQENEELKARMDKHM----AISRQLSTEQAV 1208
Cdd:pfam01576 446 SSLLneaEGKNIKLSKDvsslESQLQDTQELLQEETrqklNLSTRLRQLEDERNSLQEQLEEEEeakrNVERQLSTLQAQ 525
|
....*..
gi 50348611 1209 LQESLEK 1215
Cdd:pfam01576 526 LSDMKKK 532
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
944-1136 |
1.39e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 944 LSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQA-----EKTERENRLKEFyTREYEKL 1018
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqELEALEAELAEL-PERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1019 RdtyiEEAEKYKmQLQEQFDNLNAAHETSKLEIEashsEKLELLKKAYEASLSEIKKghEIEKksledlLSEKQESLEKQ 1098
Cdd:COG4717 152 E----ERLEELR-ELEEELEELEAELAELQEELE----ELLEQLSLATEEELQDLAE--ELEE------LQQRLAELEEE 214
|
170 180 190
....*....|....*....|....*....|....*....
gi 50348611 1099 INDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYL 1136
Cdd:COG4717 215 LEEAQEELEELEEELEQlENELEAAALEERLKEARLLLL 253
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1023-1265 |
2.15e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1023 IEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEkLELLKKAYEASLSEIKKgheiekksledlLSEKQESLEKQINDL 1102
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ-LAALERRIAALARRIRA------------LEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1103 KSENDALNEKLKSEEQKRRAREKANLKNPQIMYLE------------QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 1170
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllspedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1171 NTALVDKLKRFQQENEE----LKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLsmenEELLWKLHNGDLCSPKRSP 1246
Cdd:COG4942 169 LEAERAELEALLAELEEeraaLEALKAERQKLLARLEKELAELAAELAELQQEAEEL----EALIARLEAEAAAAAERTP 244
|
250
....*....|....*....
gi 50348611 1247 TSSAiplqsPRNSGSFPSP 1265
Cdd:COG4942 245 AAGF-----AALKGKLPWP 258
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
921-1126 |
2.21e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 921 QLKQLlacgNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEK 1000
Cdd:COG4942 28 ELEQL----QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1001 TERENRLKEFYT---REYEKL------------RDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLK-- 1063
Cdd:COG4942 104 EELAELLRALYRlgrQPPLALllspedfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAel 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50348611 1064 KAYEASLSEIKKgheiEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA 1126
Cdd:COG4942 184 EEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
940-1238 |
2.39e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 940 IQHLLSEREEALKQHKTLSQELVNLRGELVTASttcEKLEKARNELQTVYEAfVQQHQAEKTERENRLKEFYtREYEKLR 1019
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQAR---SELEQLEEELEELNEQ-LQAAQAELAQAQEELESLQ-EEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1020 DTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIeASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQI 1099
Cdd:COG4372 115 EE-LEELQKERQDLEQQRKQLEAQIAELQSEI-AEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1100 ND--LKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNntalVDK 1177
Cdd:COG4372 193 NRnaEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL----AIL 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50348611 1178 LKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLWKLHNGD 1238
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLE 329
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
990-1224 |
2.50e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 990 EAFVQQHQAEKTERENRLKEFYTREYEKLRDTY-------IEEAEKYKMQLQEQFDNLNAAHE-TSKLEIEASHSEKLEL 1061
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALglppdlsPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAAL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1062 LKKAYEASLSEIKKGHEIEKKSLEdlLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREkanlknpqimyLEQELE 1141
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQE--LKEELEELEEQLEELLGELEELLEALDEEELEEELEE-----------LEEELE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1142 SLKAVLEIKNEKLHQQDIKLMKMEklvdNNTALVDKLKRFQQENEELKARMDKHMAisrqLSTEQAVLQESL-----EKE 1216
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLE----EDGELAELLQELEELKAELRELAEEWAA----LKLALELLEEAReeyreERL 514
|
....*...
gi 50348611 1217 SKVNKRLS 1224
Cdd:COG4717 515 PPVLERAS 522
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
941-1214 |
2.50e-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: 55.57 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 941 QHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeafvqqhqAEKTERENRLKEFYTREYEKLRD 1020
Cdd:pfam01576 22 QKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLA-----------ARKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1021 TYIEEAEKYKMQ-----LQEQFDNLNAAHEtsKLEIEASHSE----KLELLKKAYEASLSEIKKgheiEKKSLEDLLSE- 1090
Cdd:pfam01576 91 SQQLQNEKKKMQqhiqdLEEQLDEEEAARQ--KLQLEKVTTEakikKLEEDILLLEDQNSKLSK----ERKLLEERISEf 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1091 -----KQESLEKQINDLKSENDA----LNEKLKSEEQKRRAREKANLK--------NPQIMYLEQELESLKAVLEIKNEK 1153
Cdd:pfam01576 165 tsnlaEEEEKAKSLSKLKNKHEAmisdLEERLKKEEKGRQELEKAKRKlegestdlQEQIAELQAQIAELRAQLAKKEEE 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50348611 1154 LHQqdiKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLE 1214
Cdd:pfam01576 245 LQA---ALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELE 302
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1019-1230 |
2.73e-07 |
|
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: 55.45 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1019 RDTYIEEA---EKYKMQLQEQFDNLNAA-----------HETSK----LEIEASHSEKLellkKAYEASLSEIKKG-HEI 1079
Cdd:TIGR02168 157 RRAIFEEAagiSKYKERRKETERKLERTrenldrledilNELERqlksLERQAEKAERY----KELKAELRELELAlLVL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1080 EKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpqimyLEQELESL-KAVLEIKNEklhQQD 1158
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE----------LEEEIEELqKELYALANE---ISR 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50348611 1159 IKLMKMEkLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEEL 1230
Cdd:TIGR02168 300 LEQQKQI-LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
941-1231 |
3.20e-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: 55.03 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 941 QHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEklrd 1020
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE---- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1021 tyIEEAEKYKMQLQEQFDNLNAahetsklEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLE------DLLSEKQES 1094
Cdd:TIGR04523 276 --LEQNNKKIKELEKQLNQLKS-------EISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISqnnkiiSQLNEQISQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1095 LEKQINDLKSENDALN----------EKLKSEEQKRRaREKANLKNpQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKM 1164
Cdd:TIGR04523 347 LKKELTNSESENSEKQreleekqneiEKLKKENQSYK-QEIKNLES-QINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50348611 1165 EKLVDN----NTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKE----SKVNKRLSMENEELL 1231
Cdd:TIGR04523 425 EKEIERlketIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIkqnlEQKQKELKSKEKELK 499
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
997-1231 |
3.55e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 997 QAEKTERenrlkefytreYEKLRdtyiEEAEKYKMQLQ-EQFDNLNAAHETSKLEIEAshsekLELLKKAYEASLSEIKK 1075
Cdd:COG1196 208 QAEKAER-----------YRELK----EELKELEAELLlLKLRELEAELEELEAELEE-----LEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1076 GHEIEKKSLEDLlsekqeslEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpQIMYLEQELESLKAVL-------- 1147
Cdd:COG1196 268 ELEELRLELEEL--------ELELEEAQAEEYELLAELARLEQDIARLEE------RRRELEERLEELEEELaeleeele 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1148 -------EIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVN 1220
Cdd:COG1196 334 eleeeleELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
250
....*....|.
gi 50348611 1221 KRLSMENEELL 1231
Cdd:COG1196 414 ERLERLEEELE 424
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
902-1231 |
4.66e-07 |
|
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: 54.34 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 902 TLELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREE--ALKQHKTLS-QELVNLRGELVTASTTCEKL 978
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtKFKNNKEVElEELKKILAEDEKLLDEKKQF 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 979 EKARNELQTVYEAFV---QQHQAEKTERENRL------KEFYTREYEKLRdtyiEEAEKYKMQLQE--------QFDNLN 1041
Cdd:pfam05483 428 EKIAEELKGKEQELIfllQAREKEIHDLEIQLtaiktsEEHYLKEVEDLK----TELEKEKLKNIEltahcdklLLENKE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1042 AAHETSKLEIE-ASHSEKLELLKKAYEASLSEIKKGHEIEKKsLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKR 1120
Cdd:pfam05483 504 LTQEASDMTLElKKHQEDIINCKKQEERMLKQIENLEEKEMN-LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEV 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1121 RAREKA---------NL------KNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKME-KLVDNNTALVDKLKRFQQE 1184
Cdd:pfam05483 583 LKKEKQmkilenkcnNLkkqienKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElELASAKQKFEEIIDNYQKE 662
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 50348611 1185 NEELKARMDKHMAisrQLSTEQAVLQESLEKESKVNKRLSMENEELL 1231
Cdd:pfam05483 663 IEDKKISEEKLLE---EVEKAKAIADEAVKLQKEIDKRCQHKIAEMV 706
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
940-1224 |
5.19e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 940 IQHLLSEREEALKQHKTLSQELVNLRGELVTAS------TTCEKLEKARNELQtvyeafvqQHQAEKTEREnrlkefyTR 1013
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkELAEQLKELEEKLK--------KYNLEELEKK-------AE 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1014 EYEKLRdtyiEEAEKYKmqlqeqfdnlnaahetSKLEIEASHSEKLELLKKAYEASLSEIKKGHEiEKKSLEDLLSEK-- 1091
Cdd:PRK03918 526 EYEKLK----EKLIKLK----------------GEIKSLKKELEKLEELKKKLAELEKKLDELEE-ELAELLKELEELgf 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1092 --QESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLM--KMEKL 1167
Cdd:PRK03918 585 esVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeEYEEL 664
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 50348611 1168 VDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLS 1224
Cdd:PRK03918 665 REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1091-1216 |
7.59e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1091 KQESLEKQINDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMK------ 1163
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDAlQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1164 ---------------------------MEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKE 1216
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
900-1215 |
8.17e-07 |
|
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: 53.67 E-value: 8.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 900 EKTLELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLE 979
Cdd:pfam10174 363 KKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLE 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 980 KARNELQTVYEAFvqQHQAEKTERENRlkefytreyeklrdtyiEEAEKYKMQLQEQFDNLNAAHeTSKLEIEAShseKL 1059
Cdd:pfam10174 443 EALSEKERIIERL--KEQREREDRERL-----------------EELESLKKENKDLKEKVSALQ-PELTEKESS---LI 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1060 ELLKKAYEASLSEIKKGHEIekKSLEDLLSEKQESLEKQINDL-KSENDALNEKLKSE--EQKRRAREKANLKNPQIMYL 1136
Cdd:pfam10174 500 DLKEHASSLASSGLKKDSKL--KSLEIAVEQKKEECSKLENQLkKAHNAEEAVRTNPEinDRIRLLEQEVARYKEESGKA 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1137 EQELESLKAVL-EIKNEKlHQQDIKLMKMEKL----VDNNTALVDKLKRFQQEN--------EELKARMDKHMAISRQLS 1203
Cdd:pfam10174 578 QAEVERLLGILrEVENEK-NDKDKKIAELESLtlrqMKEQNKKVANIKHGQQEMkkkgaqllEEARRREDNLADNSQQLQ 656
|
330
....*....|..
gi 50348611 1204 TEQavLQESLEK 1215
Cdd:pfam10174 657 LEE--LMGALEK 666
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
944-1229 |
9.31e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 9.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 944 LSEREEALKQHKT-LSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFytREYEKLRDTY 1022
Cdd:COG1340 6 LSSSLEELEEKIEeLREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKV--KELKEERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1023 IEEAEKYKMQLqEQFDNLNAAHETSKLEIEAshseklelLKKAYEaslseikkghEIEKKSL-EDLLSEKQESLEKQIND 1101
Cdd:COG1340 84 NEKLNELREEL-DELRKELAELNKAGGSIDK--------LRKEIE----------RLEWRQQtEVLSPEEEKELVEKIKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1102 LKSEndaLNEKLKSEEQKRRAREkanlknpqimyLEQELESLKavleIKNEKLHQQDIKLM--------KMEKLVDNNTA 1173
Cdd:COG1340 145 LEKE---LEKAKKALEKNEKLKE-----------LRAELKELR----KEAEEIHKKIKELAeeaqelheEMIELYKEADE 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 50348611 1174 LVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEE 1229
Cdd:COG1340 207 LRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
939-1188 |
1.07e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.43 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 939 VIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARnelqtvyeaFVQQHQAEKTERENRLKEF-YTREYEK 1017
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKE---------LLASRQLALQKMQSEKEQLtYWKEMLA 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1018 LRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQ--ESL 1095
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQtgAEL 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1096 EKQINDLKSENDALNE-----KLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 1170
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEdthllKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
250
....*....|....*...
gi 50348611 1171 NTALVDKLKRFQQENEEL 1188
Cdd:TIGR00618 861 LAQLTQEQAKIIQLSDKL 878
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
976-1162 |
1.22e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 976 EKLEKARNELQTVYEAFvqqhqAEKTERENRLKEfytrEYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIE-AS 1054
Cdd:COG4717 74 KELEEELKEAEEKEEEY-----AELQEELEELEE----ELEELEAE-LEELREELEKLEKLLQLLPLYQELEALEAElAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1055 HSEKLELLKKAYEA------SLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKanl 1128
Cdd:COG4717 144 LPERLEELEERLEElreleeELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE--- 220
|
170 180 190
....*....|....*....|....*....|....*.
gi 50348611 1129 knpQIMYLEQELESLKAVLEI--KNEKLHQQDIKLM 1162
Cdd:COG4717 221 ---ELEELEEELEQLENELEAaaLEERLKEARLLLL 253
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1034-1184 |
1.23e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 52.28 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1034 QEQFDNLNA--AHETSKLEIEASHSEKLELLKKAYEASLSEIkkghEIEKKSLEDLLSEkqesLEKQINDLKSENDALNE 1111
Cdd:PRK09039 52 DSALDRLNSqiAELADLLSLERQGNQDLQDSVANLRASLSAA----EAERSRLQALLAE----LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50348611 1112 KLKSEEQ-KRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKM-EKLvdnNTALVDK---LKRFQQE 1184
Cdd:PRK09039 124 ELDSEKQvSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLgRRL---NVALAQRvqeLNRYRSE 198
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1023-1183 |
1.36e-06 |
|
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: 51.60 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1023 IEEAEKYKMQLQEQFDNLNAAHETSKleieaSHSEKLELLKKAYEASLSeiKKGHEIEKKSLEDLLSEKQESLEKQINDL 1102
Cdd:cd22656 127 LKEAKKYQDKAAKVVDKLTDFENQTE-----KDQTALETLEKALKDLLT--DEGGAIARKEIKDLQKELEKLNEEYAAKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1103 KSENDALNEKLKSEEQKRRAREK---------ANLKN------PQIMYLEQ----------ELESLKAVLEIKNEKLHQQ 1157
Cdd:cd22656 200 KAKIDELKALIADDEAKLAAALRliadltaadTDLDNllaligPAIPALEKlqgawqaiatDLDSLKDLLEDDISKIPAA 279
|
170 180
....*....|....*....|....*.
gi 50348611 1158 DIKLMKMEKLVDNNTALVDKLKRFQQ 1183
Cdd:cd22656 280 ILAKLELEKAIEKWNELAEKADKFRQ 305
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1006-1230 |
1.61e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1006 RLKEFYTREYEKLRDTYIEEAEKykMQLqeqFDNLNAAHETSKLE-IEAshsekleLLKKAYEASLSEIKKG----HEIE 1080
Cdd:COG4717 2 KIKELEIYGFGKFRDRTIEFSPG--LNV---IYGPNEAGKSTLLAfIRA-------MLLERLEKEADELFKPqgrkPELN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1081 KKSLEDLLSEKQE--SLEKQINDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYLE--QELESLKAVLEIKNEKLH 1155
Cdd:COG4717 70 LKELKELEEELKEaeEKEEEYAELQEELEELEEELEElEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50348611 1156 QQDIKLMKMEklvdnntALVDKLKRFQQENEELKARMDKHMAiSRQLSTEQAvLQESLEKESKVNKRLSMENEEL 1230
Cdd:COG4717 150 ELEERLEELR-------ELEEELEELEAELAELQEELEELLE-QLSLATEEE-LQDLAEELEELQQRLAELEEEL 215
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
982-1145 |
1.69e-06 |
|
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: 50.69 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 982 RNELQTVYEafVQQHQAEKTERENRLKEFyTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAshsekLEL 1061
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKEL-PAELAELEDE-LAALEARLEAAKTELEDLEKEIKRLELEIEE-----VEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1062 LKKAYEASLSEIKK-------GHEIE-----KKSLEDLLSE---KQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA 1126
Cdd:COG1579 74 RIKKYEEQLGNVRNnkeyealQKEIEslkrrISDLEDEILElmeRIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170
....*....|....*....
gi 50348611 1127 nlknpqimyLEQELESLKA 1145
Cdd:COG1579 154 ---------LEAELEELEA 163
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1012-1150 |
1.96e-06 |
|
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: 51.17 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1012 TREYEKLRDtYIEEAEKYKMQLQEQFDNLNaahetSKLEIEASHSEKLE-----LLKKAYEAsLSEIKKGHEIEKKSLED 1086
Cdd:smart00787 157 KEDYKLLMK-ELELLNSIKPKLRDRKDALE-----EELRQLKQLEDELEdcdptELDRAKEK-LKKLLQEIMIKVKKLEE 229
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50348611 1087 LLSEKQEsLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKnpQIMYLEQELESLKAVLEIK 1150
Cdd:smart00787 230 LEEELQE-LESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK--EIEKLKEQLKLLQSLTGWK 290
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
940-1181 |
2.00e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.33 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 940 IQHLLSEREEALKQHKTLSQELV-------NLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYT 1012
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLKETIIknnseikDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1013 REYEklrdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE-----------LLKKAYEASLSEIKK-----G 1076
Cdd:TIGR04523 494 KEKE------LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEkeskisdledeLNKDDFELKKENLEKeidekN 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1077 HEIEK-----KSLEDLLSEKQE---SLEKQINDLKSEndaLNEKLKSEEQKRRAREKANLKNpqimyleQELESLKAVLE 1148
Cdd:TIGR04523 568 KEIEElkqtqKSLKKKQEEKQElidQKEKEKKDLIKE---IEEKEKKISSLEKELEKAKKEN-------EKLSSIIKNIK 637
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 50348611 1149 IKNEKLHQQdIKLMKME---------KLVDNNTALVDKLKRF 1181
Cdd:TIGR04523 638 SKKNKLKQE-VKQIKETikeirnkwpEIIKKIKESKTKIDDI 678
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
976-1234 |
2.33e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 976 EKLEKARNELQTVyeafvqqhQAEKTERENRLKEfYTREyeklrdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASh 1055
Cdd:TIGR02169 681 ERLEGLKRELSSL--------QSELRRIENRLDE-LSQE--------LSDASRKIGEIEKEIEQLEQEEEKLKERLEEL- 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1056 seklellkkayEASLSEIKKGHEIEKKSLEDLLSEKQEsLEKQINDLKSENDALNEKLkSEEQKRRAREKANLKNPQIMY 1135
Cdd:TIGR02169 743 -----------EEDLSSLEQEIENVKSELKELEARIEE-LEEDLHKLEEALNDLEARL-SHSRIPEIQAELSKLEEEVSR 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1136 LEQELESLKAVLeikNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKAR-------MDKHMAISRQLSTEQAV 1208
Cdd:TIGR02169 810 IEARLREIEQKL---NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKkeeleeeLEELEAALRDLESRLGD 886
|
250 260
....*....|....*....|....*.
gi 50348611 1209 LQESLEKESKVNKRLSMENEELLWKL 1234
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQI 912
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
913-1222 |
2.55e-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: 51.88 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 913 ENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEkarnELQTVYEAF 992
Cdd:COG5185 160 IIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAK----EIINIEEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 993 VQQhqaEKTERENRLKEFYTREYEKLrdtyIEEAEKYKM----QLQEQFDNLNAAHETSKLEIEaSHSEKLELLKKAYEA 1068
Cdd:COG5185 236 KGF---QDPESELEDLAQTSDKLEKL----VEQNTDLRLeklgENAESSKRLNENANNLIKQFE-NTKEKIAEYTKSIDI 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1069 SLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLE 1148
Cdd:COG5185 308 KKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIE 387
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50348611 1149 IKNEKLHQQDIKLMKMEKlvDNNTALVDKLKRFQQENEELKARMDKhmaISRQLSTEQAVLQESLEKESKVNKR 1222
Cdd:COG5185 388 STKESLDEIPQNQRGYAQ--EILATLEDTLKAADRQIEELQRQIEQ---ATSSNEEVSKLLNELISELNKVMRE 456
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1057-1223 |
2.59e-06 |
|
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: 49.92 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1057 EKLELLKK--AYEASLSEIK---KGHEIEKKSLEDLLSEKQESLEK---QINDLKSENDALNEKLKSEEQKR-RAREK-A 1126
Cdd:COG1579 4 EDLRALLDlqELDSELDRLEhrlKELPAELAELEDELAALEARLEAaktELEDLEKEIKRLELEIEEVEARIkKYEEQlG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1127 NLKNP-QIMYLEQELESLKAVLEIKNEKLhqqdIKLM-KMEKLVDNNTALVDKLKRFQQENEELKARMDKhmAISRQLST 1204
Cdd:COG1579 84 NVRNNkEYEALQKEIESLKRRISDLEDEI----LELMeRIEELEEELAELEAELAELEAELEEKKAELDE--ELAELEAE 157
|
170
....*....|....*....
gi 50348611 1205 EQAVLQESLEKESKVNKRL 1223
Cdd:COG1579 158 LEELEAEREELAAKIPPEL 176
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
939-1230 |
3.00e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 939 VIQHLLSEREEALK----QHKTLSQELVNLRGELVTASTTCEKLEKARNELQTvyEAFVQQHQAEKTERE-NRLKEfYTR 1013
Cdd:TIGR04523 58 NLDKNLNKDEEKINnsnnKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS--EIKNDKEQKNKLEVElNKLEK-QKK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1014 EYEKLRDTYIEEAEKykmqLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAY--EASLSEIKKGHEIEKKSLEDL--LS 1089
Cdd:TIGR04523 135 ENKKNIDKFLTEIKK----KEKELEKLNNKYNDLKKQKEELENELNLLEKEKLniQKNIDKIKNKLLKLELLLSNLkkKI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1090 EKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA-NLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLV 1168
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEiSNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50348611 1169 DNNTALVDKLKRFQQEN------EELKARMDKHMAISRQLS-TEQAV--LQESLEKESKVNKRLSMENEEL 1230
Cdd:TIGR04523 291 NQLKSEISDLNNQKEQDwnkelkSELKNQEKKLEEIQNQISqNNKIIsqLNEQISQLKKELTNSESENSEK 361
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
955-1237 |
4.53e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 51.33 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 955 KTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFV--QQHQ------------------AE-------------KT 1001
Cdd:pfam01576 548 KRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLvdLDHQrqlvsnlekkqkkfdqmlAEekaisaryaeerdRA 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1002 ERENRLKEF----YTREYEKLRDTyIEEAEKYKMQLQEQFDNL--------NAAH--ETSKLEIEASHSE---KLELL-- 1062
Cdd:pfam01576 628 EAEAREKETralsLARALEEALEA-KEELERTNKQLRAEMEDLvsskddvgKNVHelERSKRALEQQVEEmktQLEELed 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1063 --------KKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDalneklksEEQKRRAREKANLKNpqim 1134
Cdd:pfam01576 707 elqatedaKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELE--------DERKQRAQAVAAKKK---- 774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1135 yLEQELESLKAVLEIKNeKLHQQDIKLMKmeklvdnntALVDKLKRFQQENEELKARMDKHMAISRQ-------LSTEQA 1207
Cdd:pfam01576 775 -LELDLKELEAQIDAAN-KGREEAVKQLK---------KLQAQMKDLQRELEEARASRDEILAQSKEsekklknLEAELL 843
|
330 340 350
....*....|....*....|....*....|
gi 50348611 1208 VLQESLEKESKVNKRLSMENEELLWKLHNG 1237
Cdd:pfam01576 844 QLQEDLAASERARRQAQQERDELADEIASG 873
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
940-1161 |
5.13e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 940 IQHLLSEREEALKQHKTLSQELVNLR---GELVTASTTCEKLEKARNELQtvyeaFVQQHQAEKTERENRLKEfYTREYE 1016
Cdd:COG1340 73 VKELKEERDELNEKLNELREELDELRkelAELNKAGGSIDKLRKEIERLE-----WRQQTEVLSPEEEKELVE-KIKELE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1017 KLrdtyIEEAEKyKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLS---------EIKK-----GHEIEKK 1082
Cdd:COG1340 147 KE----LEKAKK-ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEmielykeadELRKeadelHKEIVEA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1083 SLE-DLLSEKQESLEKQINDLKSENDALNEKLKsEEQKRRAREKANLKNPQIMyleqelESLKavleiKNEKLHQQDIKL 1161
Cdd:COG1340 222 QEKaDELHEEIIELQKELRELRKELKKLRKKQR-ALKREKEKEELEEKAEEIF------EKLK-----KGEKLTTEELKL 289
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
976-1156 |
6.57e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 976 EKLEKARNELQTVY--EAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLnaAHETSKLEIEA 1053
Cdd:COG4717 49 ERLEKEADELFKPQgrKPELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEEL--REELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1054 SHSEKLELLKKAyEASLSEIKKGHEIEKKSLEDL--LSEKQESLEKQINDLKSENDALNEK--LKSEEQKRRAREKANLK 1129
Cdd:COG4717 126 QLLPLYQELEAL-EAELAELPERLEELEERLEELreLEEELEELEAELAELQEELEELLEQlsLATEEELQDLAEELEEL 204
|
170 180
....*....|....*....|....*..
gi 50348611 1130 NPQIMYLEQELESLKAVLEIKNEKLHQ 1156
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQ 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
955-1193 |
6.83e-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: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 955 KTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFvqQHQAEKTERENRLKEfYTREYEKLRDTY--IEEAEKYKMQ 1032
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREAL--QRLAEYSWDEIDVAS-AEREIAELEAELerLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1033 LQEQFDNLNAAHETSKLEIEASHSEK---------LELLKKAYEASLSEIKKGHEIEKKSL--EDLLSEKQESLEKQI-N 1100
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIgrlekeleqAEEELDELQDRLEAAEDLARLELRALleERFAAALGDAVERELrE 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1101 DLKSENDALNEKLKSEEQK-RRAREKANLKNPQIMY-LEQELESLKAVLE----IKNEKL--HQQDIKLMKMEKLVDNNT 1172
Cdd:COG4913 770 NLEERIDALRARLNRAEEElERAMRAFNREWPAETAdLDADLESLPEYLAlldrLEEDGLpeYEERFKELLNENSIEFVA 849
|
250 260
....*....|....*....|.
gi 50348611 1173 ALVDKLKRfqqENEELKARMD 1193
Cdd:COG4913 850 DLLSKLRR---AIREIKERID 867
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
946-1231 |
9.14e-06 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 49.68 E-value: 9.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 946 EREEALKQHKTL-SQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQ---------HQAEKTERENRLKEFYTREY 1015
Cdd:pfam15742 41 GKNLDLKQHNSLlQEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKirelelevlKQAQSIKSQNSLQEKLAQEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1016 EKLRDtyieeAEKYKMQLQEQfdnLNAAHETSKLEIEASHSEKLEllKKAYEASLSEIK-KGHEIEKKSLEDLLSEKQES 1094
Cdd:pfam15742 121 SRVAD-----AEEKILELQQK---LEHAHKVCLTDTCILEKKQLE--ERIKEASENEAKlKQQYQEEQQKRKLLDQNVNE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1095 LEKQINDLKSENDAL----------------------NEKLKSEEQKRRAREKANlknpQIMYLEQELESLKAVLEI--- 1149
Cdd:pfam15742 191 LQQQVRSLQDKEAQLemtnsqqqlriqqqeaqlkqleNEKRKSDEHLKSNQELSE----KLSSLQQEKEALQEELQQvlk 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1150 --------KNEKLHQQDIKLMKMEKlvdnntalvdklkRFQQENEELKARMdkhmaisRQLSTEQAVLQESLEKESKVNK 1221
Cdd:pfam15742 267 qldvhvrkYNEKHHHHKAKLRRAKD-------------RLVHEVEQRDERI-------KQLENEIGILQQQSEKEKAFQK 326
|
330
....*....|
gi 50348611 1222 RLSMENEELL 1231
Cdd:pfam15742 327 QVTAQNEILL 336
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
927-1210 |
1.05e-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: 50.12 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 927 ACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASttcEKLEKARNELQTVYEAFVQQHQaektereNR 1006
Cdd:pfam15921 199 ASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVE---DQLEALKSESQNKIELLLQQHQ-------DR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1007 LKEFYTrEYEKLRDTYIEEAEKYKMQ----------LQEQFDNLNAAHETSKLEIEASHSE---KLELLKKAYEASLSEI 1073
Cdd:pfam15921 269 IEQLIS-EHEVEITGLTEKASSARSQansiqsqleiIQEQARNQNSMYMRQLSDLESTVSQlrsELREAKRMYEDKIEEL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1074 KK-----GHEI------------EKKSLEDLLS---------EKQESLEKQ---------------INDLKSEND----- 1107
Cdd:pfam15921 348 EKqlvlaNSELtearterdqfsqESGNLDDQLQklladlhkrEKELSLEKEqnkrlwdrdtgnsitIDHLRRELDdrnme 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1108 -----ALNEKLKSEEQKRRAREKANLKNP-----QIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLV-DNNTALVD 1176
Cdd:pfam15921 428 vqrleALLKAMKSECQGQMERQMAAIQGKnesleKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVsDLTASLQE 507
|
330 340 350
....*....|....*....|....*....|....*..
gi 50348611 1177 KLKRFQQENEE---LKARMDKHMAISRQLSTEQAVLQ 1210
Cdd:pfam15921 508 KERAIEATNAEitkLRSRVDLKLQELQHLKNEGDHLR 544
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
949-1229 |
1.08e-05 |
|
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: 49.97 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 949 EALKQHKTLSQELVNL--RGELVTASTTC------EKLEKARNELQTVYEAFVQQHQAEkterenrlkEFYTREYEKLrd 1020
Cdd:TIGR00618 184 MEFAKKKSLHGKAELLtlRSQLLTLCTPCmpdtyhERKQVLEKELKHLREALQQTQQSH---------AYLTQKREAQ-- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1021 tyiEEAEKYKMQLQEQ------FDNLNAAHETSKLEIE--------ASHSEKLELLKKAYEASLSEIKKgheiEKKSLED 1086
Cdd:TIGR00618 253 ---EEQLKKQQLLKQLrarieeLRAQEAVLEETQERINrarkaaplAAHIKAVTQIEQQAQRIHTELQS----KMRSRAK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1087 LLSEKQeSLEKQINDLKSENDALNEKLKSEEQKRRAREKANLK-----------------NPQIMYLEQELESLKAVLEI 1149
Cdd:TIGR00618 326 LLMKRA-AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIreiscqqhtltqhihtlQQQKTTLTQKLQSLCKELDI 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1150 KNEKLHQQDIKLMKME----KLVDNNTALVDKLKRFQQ--------------ENEELKARMDKHMAISRQLSTEQAVLQE 1211
Cdd:TIGR00618 405 LQREQATIDTRTSAFRdlqgQLAHAKKQQELQQRYAELcaaaitctaqceklEKIHLQESAQSLKEREQQLQTKEQIHLQ 484
|
330
....*....|....*...
gi 50348611 1212 SLEKESKVNKRLSMENEE 1229
Cdd:TIGR00618 485 ETRKKAVVLARLLELQEE 502
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1005-1156 |
1.30e-05 |
|
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: 47.59 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1005 NRLKEFY---TREYEKLRDTYieEAEKYKMQLQEQfDNLNAAHETSKlEIEaSHSEKLE-LLKKAYEasLSEIKKGHEIE 1080
Cdd:pfam13851 11 NEIKNYYndiTRNNLELIKSL--KEEIAELKKKEE-RNEKLMSEIQQ-ENK-RLTEPLQkAQEEVEE--LRKQLENYEKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1081 KKSLEDLlSEKQESLEKQINDLKSENDALNEKLKSEEQKRRA------------REKANLKNpqiMYLEQELESLKAVLE 1148
Cdd:pfam13851 84 KQSLKNL-KARLKVLEKELKDLKWEHEVLEQRFEKVERERDElydkfeaaiqdvQQKTGLKN---LLLEKKLQALGETLE 159
|
....*...
gi 50348611 1149 IKNEKLHQ 1156
Cdd:pfam13851 160 KKEAQLNE 167
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
978-1202 |
1.35e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 48.76 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 978 LEKARNELQTVYEAFVQQHQAEkterENRLKEFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHET----------- 1046
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAE----PSRLYSLYEKEIEDLRRQ-LDTLTVERARLQLELDNLRLAAEDfrqkyedelnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1047 --------------------SKLEIEA---SHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQEsLEKQINDLK 1103
Cdd:pfam00038 98 rtsaendlvglrkdldeatlARVDLEAkieSLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLD-LTSALAEIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1104 SENDALNEKLKSE--------------------EQKRRAREKANLKNPQIMYLEQELESL---KAVLEIKNEKLHQQDIK 1160
Cdd:pfam00038 177 AQYEEIAAKNREEaeewyqskleelqqaaarngDALRSAKEEITELRRTIQSLEIELQSLkkqKASLERQLAETEERYEL 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 50348611 1161 LMKM--EKLVDNNTALV---DKLKRFQQENEEL---KARMDKHMAISRQL 1202
Cdd:pfam00038 257 QLADyqELISELEAELQetrQEMARQLREYQELlnvKLALDIEIATYRKL 306
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1019-1231 |
1.43e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1019 RDTYIEEAEKYKMQLQEQFDNLNAAHEtsklEIEASHSEKLELLKKAyEASLSEIKKGHEIEKKSLEDLlSEKQESLEKQ 1098
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALA----ELRKELEELEEELEQL-RKELEELSRQISALRKDLARL-EAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1099 INDLKSENDALNEKLKSEEQKRrarEKANlknPQIMYLEQELESLKAV--------------LEIKNEKLHQQDIKLMKM 1164
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERL---EEAE---EELAEAEAEIEELEAQieqlkeelkalreaLDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50348611 1165 EKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELL 1231
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1013-1207 |
1.46e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1013 REYEKLRDTYIEEAEKykmqlqeqfdnlNAAHETSKLEIEAShsEKLELLKKAYEASLSEIKKghEIEKksLEDLLSEKQ 1092
Cdd:PRK12704 34 KEAEEEAKRILEEAKK------------EAEAIKKEALLEAK--EEIHKLRNEFEKELRERRN--ELQK--LEKRLLQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1093 ESLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpqimyLEQELESLKAVLEIKNEK---LHQQDIKLMKMEKLVD 1169
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKELEQKQQELEK----------KEEELEELIEEQLQELERisgLTAEEAKEILLEKVEE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 50348611 1170 NNTAlvDKLKRFQQENEELKARMDKH------MAISRqLSTEQA 1207
Cdd:PRK12704 166 EARH--EAAVLIKEIEEEAKEEADKKakeilaQAIQR-CAADHV 206
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
932-1194 |
1.72e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 932 KFEALTVVIQHLLSEREEALKQHKTLSQELVNLRG---ELVtasttcEKLEKARNELQTVYEAfVQQHQAEKTERENRLK 1008
Cdd:COG1340 16 KIEELREEIEELKEKRDELNEELKELAEKRDELNAqvkELR------EEAQELREKRDELNEK-VKELKEERDELNEKLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1009 EFYT--REYEKLRDTYIEEAEKYKmQLQEQFDNLNAAHETSKLEIEAshsEKlELLKK--AYEASLSEIKKGHEIEKKSL 1084
Cdd:COG1340 89 ELREelDELRKELAELNKAGGSID-KLRKEIERLEWRQQTEVLSPEE---EK-ELVEKikELEKELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1085 EDL-----LSEKQESLEKQINDLKSENDALNEKLKSEEQKR-RAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQD 1158
Cdd:COG1340 164 ELRaelkeLRKEAEEIHKKIKELAEEAQELHEEMIELYKEAdELRKEADELHKEIVEAQEKADELHEEIIELQKELRELR 243
|
250 260 270
....*....|....*....|....*....|....*.
gi 50348611 1159 IKLMKMEKlVDNNTALVDKLKRFQQENEELKARMDK 1194
Cdd:COG1340 244 KELKKLRK-KQRALKREKEKEELEEKAEEIFEKLKK 278
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1059-1234 |
1.80e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1059 LELLKKAYEaSLSEIKKGHEIEKKSLEDLLS----------EKQESLE---KQINDLKSENDALNEKL-KSEEQKRR--- 1121
Cdd:PRK03918 157 LDDYENAYK-NLGEVIKEIKRRIERLEKFIKrtenieelikEKEKELEevlREINEISSELPELREELeKLEKEVKElee 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1122 AREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNntalVDKLKRFQQENEELKARMDKHMAISRQ 1201
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE----LKELKEKAEEYIKLSEFYEEYLDELRE 311
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 50348611 1202 LSTE-----------QAVLQESLEKESKVNKrLSMENEELLWKL 1234
Cdd:PRK03918 312 IEKRlsrleeeingiEERIKELEEKEERLEE-LKKKLKELEKRL 354
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
871-1102 |
1.88e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.18 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 871 ALNAVEKSRQknprsLCIQPQTAPDALPPEktleLTQYKTKCENQSGFILQLKQLLACGN---TKFEALTVVIQHLLSE- 946
Cdd:COG3096 418 AVQALEKARA-----LCGLPDLTPENAEDY----LAAFRAKEQQATEEVLELEQKLSVADaarRQFEKAYELVCKIAGEv 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 947 -REEA-------LKQH---KTLSQELVNLRGELVTAsttcEKLEKARNELQTVYEAFVQQHQAEKTERENrLKEFYTREY 1015
Cdd:COG3096 489 eRSQAwqtarelLRRYrsqQALAQRLQQLRAQLAEL----EQRLRQQQNAERLLEEFCQRIGQQLDAAEE-LEELLAELE 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1016 EKLRD--TYIEEAEKYKMQLQEQFDNLNAAHEtsKLEIEASH----SEKLELLKKAYEASL---SEIKKG------HEIE 1080
Cdd:COG3096 564 AQLEEleEQAAEAVEQRSELRQQLEQLRARIK--ELAARAPAwlaaQDALERLREQSGEALadsQEVTAAmqqlleRERE 641
|
250 260
....*....|....*....|..
gi 50348611 1081 KKSLEDLLSEKQESLEKQINDL 1102
Cdd:COG3096 642 ATVERDELAARKQALESQIERL 663
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
904-1195 |
2.20e-05 |
|
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: 48.70 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 904 ELTQYKTKCENQSGFILQL--------KQLLAcGNTKFEALTVVIQHLLSEREEALKQHKTLSQElvnlrGELVTASTTC 975
Cdd:pfam06160 108 ELDELLESEEKNREEVEELkdkyrelrKTLLA-NRFSYGPAIDELEKQLAEIEEEFSQFEELTES-----GDYLEAREVL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 976 EKLEKARNELQTVYEAFVQQHQaekterenRLKEFYTREYEKLRDTYIE-EAEKYK---MQLQEQFDNLNAAHETS---- 1047
Cdd:pfam06160 182 EKLEEETDALEELMEDIPPLYE--------ELKTELPDQLEELKEGYREmEEEGYAlehLNVDKEIQQLEEQLEENlall 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1048 -KLEIEAShSEKLELLKKA----YEASLSEIKKGHEIEKKS--LEDLLS---------------------------EKQE 1093
Cdd:pfam06160 254 eNLELDEA-EEALEEIEERidqlYDLLEKEVDAKKYVEKNLpeIEDYLEhaeeqnkelkeelervqqsytlnenelERVR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1094 SLEKQINDLKSENDALNEKLKSEEQkrrarekanlknPQIMYLEQELESLKAVLEIKNEklhQQDIK--LMKMEKlvDNN 1171
Cdd:pfam06160 333 GLEKQLEELEKRYDEIVERLEEKEV------------AYSELQEELEEILEQLEEIEEE---QEEFKesLQSLRK--DEL 395
|
330 340
....*....|....*....|....
gi 50348611 1172 TALvDKLKRFQQENEELKARMDKH 1195
Cdd:pfam06160 396 EAR-EKLDEFKLELREIKRLVEKS 418
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
976-1212 |
2.69e-05 |
|
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: 48.11 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 976 EKLEKARnelqtvyeafvQQHQAEKTERENRLKEF-----YTREYEKLRDTYIEEAEKYKMQLQEqfdnlnaaHETSKLE 1050
Cdd:pfam15558 109 EKLERAR-----------QEAEQRKQCQEQRLKEKeeelqALREQNSLQLQERLEEACHKRQLKE--------REEQKKV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1051 IEASHSEKL--ELLKKAYEaslSEIKKGHEIEKKSLEDLLSEKQESLEKQIndlKSENDALNEK-LKSEEQKRRAREKAN 1127
Cdd:pfam15558 170 QENNLSELLnhQARKVLVD---CQAKAEELLRRLSLEQSLQRSQENYEQLV---EERHRELREKaQKEEEQFQRAKWRAE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1128 LKNpqimylEQELESLKAVLEIKNEKL-----HQQDIKLMKMEKLVDNNTA-----LVDKLKRFQQEN---EELKARMDK 1194
Cdd:pfam15558 244 EKE------EERQEHKEALAELADRKIqqarqVAHKTVQDKAQRARELNLEreknhHILKLKVEKEEKchrEGIKEAIKK 317
|
250
....*....|....*....
gi 50348611 1195 HMAISRQLSTE-QAVLQES 1212
Cdd:pfam15558 318 KEQRSEQISREkEATLEEA 336
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
1055-1206 |
3.26e-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: 44.86 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1055 HSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEK-QINDLKsendALNEKLKSEEQKRRAREKANLKNpQI 1133
Cdd:pfam12474 1 HQLQKEQQKDRFEQERQQLKKRYEKELEQLERQQKQQIEKLEQrQTQELR----RLPKRIRAEQKKRLKMFRESLKQ-EK 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50348611 1134 MYLEQELESLKavleikneKLHQQDIKLMKMEKLvdnntalvdKLKRFQQENEELKARMDKHMAISRQLSTEQ 1206
Cdd:pfam12474 76 KELKQEVEKLP--------KFQRKEAKRQRKEEL---------ELEQKHEELEFLQAQSEALERELQQLQNEK 131
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
944-1230 |
4.31e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.91 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 944 LSEREEALKQhKTLSQELV-----NLRGElvtASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKL 1018
Cdd:PRK04778 34 LEERKQELEN-LPVNDELEkvkklNLTGQ---SEEKFEEWRQKWDEIVTNSLPDIEEQLFEAEELNDKFRFRKAKHEINE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1019 RDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAshseklelLKKAYEaslsEIKKghEIEKKSleDLLSEKQESLEKQ 1098
Cdd:PRK04778 110 IESLLDLIEEDIEQILEELQELLESEEKNREEVEQ--------LKDLYR----ELRK--SLLANR--FSFGPALDELEKQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1099 INDLKSE---NDALNEK---LKSEEQKRRAREK-ANLKN-----PQIMY-----LEQELESLKAVL-EIKNEKLHQQDIK 1160
Cdd:PRK04778 174 LENLEEEfsqFVELTESgdyVEAREILDQLEEElAALEQimeeiPELLKelqteLPDQLQELKAGYrELVEEGYHLDHLD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1161 LMKM-----EKLVDNNTALVD-KLKRFQQENEELKARMDK------HMAISRQ-LSTEQAVLQESLEKESKVNKRLSMEN 1227
Cdd:PRK04778 254 IEKEiqdlkEQIDENLALLEElDLDEAEEKNEEIQERIDQlydileREVKARKyVEKNSDTLPDFLEHAKEQNKELKEEI 333
|
...
gi 50348611 1228 EEL 1230
Cdd:PRK04778 334 DRV 336
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
948-1120 |
4.32e-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: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 948 EEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKefytREyeklrdtyIEEAE 1027
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLE----RE--------IERLE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1028 KYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEikkgheiekKSLEDLLSEKQESLEKQINDLKSEND 1107
Cdd:COG4913 352 RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL---------EEELEALEEALAEAEAALRDLRRELR 422
|
170
....*....|...
gi 50348611 1108 ALNEKLKSEEQKR 1120
Cdd:COG4913 423 ELEAEIASLERRK 435
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
976-1207 |
4.43e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 976 EKLEKARNELQTVYEAFVQQHQAE--KTERENRLKEFYTREYEKLRDTY-----IEEAEKYK---MQLQEQFDNLNAAHE 1045
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEeaKKAEEAKIKAEELKKAEEEKKKVeqlkkKEAEEKKKaeeLKKAEEENKIKAAEE 1666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1046 TSKLEIEASHSEKL------------ELLKKAYEA-SLSEIKKGHEIEKKSLEDLLSEKQESLEKqINDLKSENDalNEK 1112
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAkkaeedekkaaeALKKEAEEAkKAEELKKKEAEEKKKAEELKKAEEENKIK-AEEAKKEAE--EDK 1743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1113 LKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIK-LMKMEKLV----DNNTALVDKLKR---FQQE 1184
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKrRMEVDKKIkdifDNFANIIEGGKEgnlVIND 1823
|
250 260
....*....|....*....|...
gi 50348611 1185 NEELKARMDKHMAISRQLSTEQA 1207
Cdd:PTZ00121 1824 SKEMEDSAIKEVADSKNMQLEEA 1846
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
904-1191 |
4.75e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 904 ELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARN 983
Cdd:COG4372 46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 984 ELQT---VYEAFVQQHQAEKTERENRLKEFYTREYEKLRDtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE 1060
Cdd:COG4372 126 DLEQqrkQLEAQIAELQSEIAEREEELKELEEQLESLQEE--LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1061 LLKKAYEASLSEIKKGHEIEKKSLE---DLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLE 1137
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEaklGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 50348611 1138 QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKAR 1191
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLA 337
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
921-1224 |
5.12e-05 |
|
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: 46.87 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 921 QLKQLLACGNT---KFEALTVVIQHLLSEREEALKQHK-------TLSQELVNLRGELVTASTTCEKLEKARNELQTVYE 990
Cdd:pfam09728 5 ELMQLLNKLDSpeeKLAALCKKYAELLEEMKRLQKDLKklkkkqdQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQNK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 991 AFVQQHQAEKTERENRLKEFYTREYEKLRD--TYIEEAEKYKMQLQEQFDNLnaahetskleieashSEKLELLKKAYEa 1068
Cdd:pfam09728 85 KLKEESKKLAKEEEEKRKELSEKFQSTLKDiqDKMEEKSEKNNKLREENEEL---------------REKLKSLIEQYE- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1069 sLSEikkgheiekKSLEDLLseKQESLEKQINDLK-SENDALNEKLKSEEQKRRAREkanlKNPQIMYLEQELESLKAVL 1147
Cdd:pfam09728 149 -LRE---------LHFEKLL--KTKELEVQLAEAKlQQATEEEEKKAQEKEVAKARE----LKAQVQTLSETEKELREQL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1148 EIKNEKLHQ-QDIkLMKMEKLVDNNTA----LVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKR 1222
Cdd:pfam09728 213 NLYVEKFEEfQDT-LNKSNEVFTTFKKemekMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEK 291
|
..
gi 50348611 1223 LS 1224
Cdd:pfam09728 292 LE 293
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
1013-1179 |
5.13e-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: 44.91 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1013 REYEKLRDTYIEEAEKYKM----QLQEQFDNLNAAHETSKLEIEAShSEKLELLKKAYEASlSEIKKGHEIEKKSLEDLL 1088
Cdd:pfam09744 10 KEFERLIDRYGEDVVKGLMpkvvNVLELLESLASRNQEHNVELEEL-REDNEQLETQYERE-KALRKRAEEELEEIEDQW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1089 SEKQESLEKQINDLKSENDALneklkseEQKRRARekanlknpqimyleqeLESLKAVLEIKNEKLHQQDIKLMKmeKLV 1168
Cdd:pfam09744 88 EQETKDLLSQVESLEEENRRL-------EADHVSR----------------LEEKEAELKKEYSKLHERETEVLR--KLK 142
|
170
....*....|.
gi 50348611 1169 DnntaLVDKLK 1179
Cdd:pfam09744 143 E----VVDRQR 149
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
1048-1193 |
7.92e-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: 43.83 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1048 KLEIEASHSEKLELLKKAYEASLSEIKKGHEIEkksledllsekqeSLEKQINDLKSENDALNEKLKseEQKRRAREKAN 1127
Cdd:pfam12718 6 KLEAENAQERAEELEEKVKELEQENLEKEQEIK-------------SLTHKNQQLEEEVEKLEEQLK--EAKEKAEESEK 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50348611 1128 LK------NPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKlvdnntalvdKLKRFQQENEELKARMD 1193
Cdd:pfam12718 71 LKtnnenlTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLER----------KVQALEQERDEWEKKYE 132
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
979-1222 |
8.34e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 979 EKARNELQTVYEAFVQQHQAEKTEREnRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEiEASHSEK 1058
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEE-RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEE 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1059 L----ELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRARE-KANLKNPQI 1133
Cdd:PTZ00121 1301 KkkadEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkKKEEAKKKA 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1134 MYLEQELESLKAVLEIKneKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQEN---EELKARM-DKHMAISRQLSTEQAVL 1209
Cdd:PTZ00121 1381 DAAKKKAEEKKKADEAK--KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkaDEAKKKAeEAKKADEAKKKAEEAKK 1458
|
250
....*....|...
gi 50348611 1210 QESLEKESKVNKR 1222
Cdd:PTZ00121 1459 AEEAKKKAEEAKK 1471
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1062-1215 |
9.27e-05 |
|
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: 44.90 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1062 LKKAYEASLSEIKKGH-EIEKKSLEDL---------LSEKQESLEKQINDLKSENDALNEKLKsEEQKRRAREKANLKNP 1131
Cdd:pfam13851 2 LMKNHEKAFNEIKNYYnDITRNNLELIkslkeeiaeLKKKEERNEKLMSEIQQENKRLTEPLQ-KAQEEVEELRKQLENY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1132 QimYLEQELESLKAVLEIKNEKL----HQQDIKLMKMEKLVDNNTALvdkLKRFQQENEELKARMD-KHMAISRQLSTeq 1206
Cdd:pfam13851 81 E--KDKQSLKNLKARLKVLEKELkdlkWEHEVLEQRFEKVERERDEL---YDKFEAAIQDVQQKTGlKNLLLEKKLQA-- 153
|
....*....
gi 50348611 1207 avLQESLEK 1215
Cdd:pfam13851 154 --LGETLEK 160
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
992-1157 |
1.04e-04 |
|
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: 45.12 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 992 FVQQHQAEKTERENrLKEFYTREYEKLRDTyieeaEKYKMQLQEQFDNLNAAHETSKLE------IEASHSEKLELLKKA 1065
Cdd:pfam17078 43 FLENLASLKHENDN-LSSMLNRKERRLKDL-----EDQLSELKNSYEELTESNKQLKKRlenssaSETTLEAELERLQIQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1066 YEASLSEIK--KGH---EIE--KKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREkaNLKNPQIMYLEQ 1138
Cdd:pfam17078 117 YDALVDSQNeyKDHyqqEINtlQESLEDLKLENEKQLENYQQRISSNDKDIDTKLDSYNNKFKNLD--NIYVNKNNKLLT 194
|
170 180
....*....|....*....|
gi 50348611 1139 ELESLKAVLEIKN-EKLHQQ 1157
Cdd:pfam17078 195 KLDSLAQLLDLPSwLNLYPE 214
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1079-1218 |
1.18e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1079 IEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSE------EQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNE 1152
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEakeeihKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50348611 1153 KLHQQDIKLMKMEKLVDNNTALVDKLkrfQQENEELKARMDKHMAISRQLSTEQA--VLQESLEKESK 1218
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKK---EEELEELIEEQLQELERISGLTAEEAkeILLEKVEEEAR 168
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1084-1234 |
1.25e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1084 LEDLLSEkqesLEKQINDLKSE-NDALN-EKLKSEEQKRRAREKANlknpQIMYLEQELESLKAVLEIKNEKLHQQDIKL 1161
Cdd:COG1196 191 LEDILGE----LERQLEPLERQaEKAERyRELKEELKELEAELLLL----KLRELEAELEELEAELEELEAELEELEAEL 262
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50348611 1162 MKMEKLVDNNTAlvdKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLWKL 1234
Cdd:COG1196 263 AELEAELEELRL---ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1082-1239 |
1.80e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1082 KSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRArekanlknpqimyleqeleslkavleiKNEKLHQQDIKL 1161
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDE---------------------------LNAQVKELREEA 59
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50348611 1162 MKMEKLVDnntALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLsmenEELLWKLHNGDL 1239
Cdd:COG1340 60 QELREKRD---ELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEI----ERLEWRQQTEVL 130
|
|
| Snf7 |
pfam03357 |
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ... |
1085-1234 |
1.81e-04 |
|
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: 43.38 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1085 EDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNpQIMYLEQELESLKAVLE-IKNEKLHQQDIKLMK 1163
Cdd:pfam03357 10 IRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEK-QLDQLDGQLSNLEQQRMaIENAKSNQEVLNAMK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1164 --------MEKLVDnntalVDKLKRFQQENEELKARMD-KHMAISRQLSTEQAVLQESLEKEskVNKRLSMENEELLWKL 1234
Cdd:pfam03357 89 qgakamkaMNKLMD-----IDKIDKLMDEIEDQMEKADeISEMLSDPLDDADEEDEEELDAE--LDALLDEIGDEESVEL 161
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1023-1236 |
1.86e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.12 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1023 IEEAEKYKMQLQEQFDNLNAAHETSKLEIEASH--SEKLELLKKAYEASLSEIK-KGHEIEKKSLEDLLSEKQESLEKQI 1099
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDleELKLQELKLKEQAKKALEYyQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1100 NDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMyLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLK 1179
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKE-NKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 50348611 1180 RFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLWKLHN 1236
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE 374
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
910-1161 |
1.89e-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: 45.98 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 910 TKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQhktLSQELVNLRGELVtasttcEKLEKARNELQTVY 989
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAE---LNQLLRTLDDQWK------EKRDELNGELSAAD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 990 EAfVQQHQAEKTERENRLKEFYTREYEKLR---------DTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE 1060
Cdd:pfam12128 315 AA-VAKDRSELEALEDQHGAFLDADIETAAadqeqlpswQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIA 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1061 LLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSE--------------EQKR------ 1120
Cdd:pfam12128 394 GIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELklrlnqatatpellLQLEnfderi 473
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 50348611 1121 -RAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKL 1161
Cdd:pfam12128 474 eRAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRL 515
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1032-1230 |
1.95e-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: 45.89 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1032 QLQEQFDNLNAAHETSKLEIEaSHSEKLELLKKAYEASLS---EIKKGHEIEK--KSLEDLLSEKQESLEKQIN---DLK 1103
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELE-HKRARIELEKKASALKRQldrESDRNQELQKriRLLEKREAEAEEALREQAElnrLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1104 SENDALNEKLKSEEQKR-RARE-KANLKNP------QIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALV 1175
Cdd:pfam05557 83 KYLEALNKKLNEKESQLaDAREvISCLKNElselrrQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQ 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 50348611 1176 DKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVnKRLSMENEEL 1230
Cdd:pfam05557 163 SSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPELEKEL-ERLREHNKHL 216
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
947-1241 |
2.20e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 947 REEALKQHKTLSQELVNLRGELV-TASTTcekleKARNELQTVYEAFVQQHQaEKTERENRLKEFYTREYEKLRDTYIEE 1025
Cdd:pfam01576 287 RNKAEKQRRDLGEELEALKTELEdTLDTT-----AAQQELRSKREQEVTELK-KALEEETRSHEAQLQEMRQKHTQALEE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1026 aekykmqLQEQFDNLN---AAHETSKLEIEASHSEKLELLKkayeaSLSEIKKGHEIEKKSLEDLLSE-----------K 1091
Cdd:pfam01576 361 -------LTEQLEQAKrnkANLEKAKQALESENAELQAELR-----TLQQAKQDSEHKRKKLEGQLQElqarlseserqR 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1092 QESLEKqINDLKSENDALNEKLKSEEQK-----------------------RRAREKANLKNpQIMYLEQELESLKAVLE 1148
Cdd:pfam01576 429 AELAEK-LSKLQSELESVSSLLNEAEGKniklskdvsslesqlqdtqellqEETRQKLNLST-RLRQLEDERNSLQEQLE 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1149 IKNEK-------LHQQDIKLMKMEKLVDNNTALVDKL----KRFQQENEELKARMDkhmaisrqlstEQAVLQESLEKEs 1217
Cdd:pfam01576 507 EEEEAkrnverqLSTLQAQLSDMKKKLEEDAGTLEALeegkKRLQRELEALTQQLE-----------EKAAAYDKLEKT- 574
|
330 340
....*....|....*....|....*
gi 50348611 1218 kvNKRLSMENEELLWKL-HNGDLCS 1241
Cdd:pfam01576 575 --KNRLQQELDDLLVDLdHQRQLVS 597
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1033-1230 |
2.27e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1033 LQE----QFDNLNAAHETSKLEIEASH----SEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESL---EKQIND 1101
Cdd:PRK05771 25 LHElgvvHIEDLKEELSNERLRKLRSLltklSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELekiEKEIKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1102 LKSENDALNEKLKSEEQKRRAREK-ANLKNPQImyLEQELESLKAVL------EIKNEKLHQQDIKLMKMEKLVDNNTAL 1174
Cdd:PRK05771 105 LEEEISELENEIKELEQEIERLEPwGNFDLDLS--LLLGFKYVSVFVgtvpedKLEELKLESDVENVEYISTDKGYVYVV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1175 VDKLKRFQQE-NEELKarmdKHMAISRQLSTE---QAVLQESLEKESKVNKRLSMENEEL 1230
Cdd:PRK05771 183 VVVLKELSDEvEEELK----KLGFERLELEEEgtpSELIREIKEELEEIEKERESLLEEL 238
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
945-1224 |
2.33e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 945 SEREEALKQHKTLSQELVN----LRGELVTASTTCEKLEKARNELqtvyEAFVQQHQAEKTERENRLKEFyTREYEKLRD 1020
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEeaesLREDADDLEERAEELREEAAEL----ESELEEAREAVEDRREEIEEL-EEEIEELRE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1021 TY------IEEAEKYKMQLQEqfdNLNAAHETSKlEIEASHSEKLELLKKAyEASLSEIKK---GHEIEKKSLEDLLSEK 1091
Cdd:PRK02224 399 RFgdapvdLGNAEDFLEELRE---ERDELREREA-ELEATLRTARERVEEA-EALLEAGKCpecGQPVEGSPHVETIEED 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1092 QE---SLEKQINDLKSENDALNEKLKSEEQ-----KRRAREKANLKNpqimyLEQELESLKAVLEIKNEKLhqqdiklmk 1163
Cdd:PRK02224 474 RErveELEAELEDLEEEVEEVEERLERAEDlveaeDRIERLEERRED-----LEELIAERRETIEEKRERA--------- 539
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50348611 1164 mEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLS 1224
Cdd:PRK02224 540 -EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA 599
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
999-1119 |
2.53e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 999 EKTERENRLKEFYTREYEKLRdtyiEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEI----- 1073
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALL----KEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELrqlqk 598
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 50348611 1074 KKGHEIEKKSLED---LLSEKQESLEKQINDLKSENDALNE----KLKSEEQK 1119
Cdd:PRK00409 599 GGYASVKAHELIEarkRLNKANEKKEKKKKKQKEKQEELKVgdevKYLSLGQK 651
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
993-1197 |
2.75e-04 |
|
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: 43.86 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 993 VQQHQAEKTERENRLKEFyTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKlEIEASHSEKLELLKKAYEASlSE 1072
Cdd:pfam00261 3 MQQIKEELDEAEERLKEA-MKKLEEAEKR-AEKAEAEVAALNRRIQLLEEELERTE-ERLAEALEKLEEAEKAADES-ER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1073 IKKGheIEKKSLEDllSEKQESLEKQINDLKSENDALNEKLKSEEQK--------RRAREKANLKNPQIMYLEQEL---- 1140
Cdd:pfam00261 79 GRKV--LENRALKD--EEKMEILEAQLKEAKEIAEEADRKYEEVARKlvvvegdlERAEERAELAESKIVELEEELkvvg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1141 ESLKAvLEIKNEKLHQQDIK-------------------------LMKMEKLVDnntALVDKLKRFQQENEELKARMDKH 1195
Cdd:pfam00261 155 NNLKS-LEASEEKASEREDKyeeqirflteklkeaetraefaersVQKLEKEVD---RLEDELEAEKEKYKAISEELDQT 230
|
..
gi 50348611 1196 MA 1197
Cdd:pfam00261 231 LA 232
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
980-1229 |
2.86e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 980 KARNELQTVYEAfvQQHQAEKTERENRLKEfytreYEKLRDTYIEEAEKYKMQLQEQfdnlnaahetskleIEASHSEKL 1059
Cdd:pfam13868 32 KRIKAEEKEEER--RLDEMMEEERERALEE-----EEEKEEERKEERKRYRQELEEQ--------------IEEREQKRQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1060 EllkkAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINdLKSENDALNEKLKSEEQKRRAREK-ANLKNpqimyleq 1138
Cdd:pfam13868 91 E----EYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQ-LREEIDEFNEEQAEWKELEKEEEReEDERI-------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1139 eLESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKAR--MDKHMAISRQLSTEQAvlqeslEKE 1216
Cdd:pfam13868 158 -LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKlyQEEQERKERQKEREEA------EKK 230
|
250
....*....|...
gi 50348611 1217 SKVNKRLSMENEE 1229
Cdd:pfam13868 231 ARQRQELQQAREE 243
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
904-1195 |
3.02e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 904 ELTQYKTKCENQSGFILQL--------KQLLAcGNTKFEALTVVIQHLLSEREEALKQHKTLSQElvnlrGELVTASttc 975
Cdd:PRK04778 127 ELQELLESEEKNREEVEQLkdlyrelrKSLLA-NRFSFGPALDELEKQLENLEEEFSQFVELTES-----GDYVEAR--- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 976 EKLEKARNELQTVyeafvqQHQAEK-----TERENRLKEfytrEYEKLRDTYIE-EAEKYK---MQLQEQFDNLNAAHET 1046
Cdd:PRK04778 198 EILDQLEEELAAL------EQIMEEipellKELQTELPD----QLQELKAGYRElVEEGYHldhLDIEKEIQDLKEQIDE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1047 -----SKLEIEAShSEKLELLKKA----YEASLSEIKKGHEIEKKS--LEDLLS-------------------------- 1089
Cdd:PRK04778 268 nlallEELDLDEA-EEKNEEIQERidqlYDILEREVKARKYVEKNSdtLPDFLEhakeqnkelkeeidrvkqsytlnese 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1090 -EKQESLEKQINDLKSENDALNEKLksEEQKRRAREkanlknpqimyLEQELESLKAVL-EIKNEklhQQDIK--LMKME 1165
Cdd:PRK04778 347 lESVRQLEKQLESLEKQYDEITERI--AEQEIAYSE-----------LQEELEEILKQLeEIEKE---QEKLSemLQGLR 410
|
330 340 350
....*....|....*....|....*....|
gi 50348611 1166 KlvDNNTALvDKLKRFQQENEELKARMDKH 1195
Cdd:PRK04778 411 K--DELEAR-EKLERYRNKLHEIKRYLEKS 437
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
1006-1149 |
4.21e-04 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 43.85 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1006 RLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSE--KLELLKKAYEASLSEIKKGHEIEK-- 1081
Cdd:PRK06669 26 RFKVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEeaKEELLKKTDEASSIIEKLQMQIEReq 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50348611 1082 -KSLEDLLSEKQESLEKQIND--LKSENDALNEKLKSEEQKRRAREKANLK-NPQIMYLEQELESLkaVLEI 1149
Cdd:PRK06669 106 eEWEEELERLIEEAKAEGYEEgyEKGREEGLEEVRELIEQLNKIIEKLIKKrEEILESSEEEIVEL--ALDI 175
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
900-1215 |
4.47e-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: 44.29 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 900 EKTLEltQYKTKCENQSGFILQLKQLLacgntkfEALTVVIQHLLSEREEALK------QHKTLSQELVNLRGELVTAST 973
Cdd:pfam05622 134 EATVE--TYKKKLEDLGDLRRQVKLLE-------ERNAEYMQRTLQLEEELKKanalrgQLETYKRQVQELHGKLSEESK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 974 TCEKLEKARNELQTVYEAFVQqhqaektERENRLKEfytreyeklRDTYIEEAEKYK-MQLQEqfdnlnaAHETSKLEIE 1052
Cdd:pfam05622 205 KADKLEFEYKKLEEKLEALQK-------EKERLIIE---------RDTLRETNEELRcAQLQQ-------AELSQADALL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1053 ASHSEKLELLkkAYEASLSEIKKghEIEKKSLED-LLSEKQE-SLEKQINDLKSENDalneklKSEEQKRRAREKANLKN 1130
Cdd:pfam05622 262 SPSSDPGDNL--AAEIMPAEIRE--KLIRLQHENkMLRLGQEgSYRERLTELQQLLE------DANRRKNELETQNRLAN 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1131 PQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKArmdkhmAISRQLSTEQAVLQ 1210
Cdd:pfam05622 332 QRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEP------KQDSNLAQKIDELQ 405
|
....*
gi 50348611 1211 ESLEK 1215
Cdd:pfam05622 406 EALRK 410
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1023-1166 |
4.67e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1023 IEEAEKYKMQLQEQFDNLnaahetskleIEASHSEKLELLKKAYEASlsEIKKGHEIEKKSLEDLLSEKQESLEKQINDL 1102
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNEL----------IASLEELERELEQKAEEAE--ALLKEAEKLKEELEEKKEKLQEEEDKLLEEA 571
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50348611 1103 KSE-NDALNE-KLKSEEQKRRAREKANLKNPQIMylEQELESLKAVLEIKNEKLHQQDIKLMKMEK 1166
Cdd:PRK00409 572 EKEaQQAIKEaKKEADEIIKELRQLQKGGYASVK--AHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
944-1216 |
7.21e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 944 LSEREEALKQHKTLSQELVNLRGELVTAsttcEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTYI 1023
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKKA----EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1024 EEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDlLSEKQESLEKQINDLK 1103
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE-EAKKAEEDKKKAEEAK 1681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1104 SENDalNEKLKSEEQKRRAREKANLKNPQimylEQELESLKAVLEIKNEKlHQQDIKLMKMEKLVDNNTALVDKLKRFQQ 1183
Cdd:PTZ00121 1682 KAEE--DEKKAAEALKKEAEEAKKAEELK----KKEAEEKKKAEELKKAE-EENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
250 260 270
....*....|....*....|....*....|....
gi 50348611 1184 ENEELKARMDKHMAISRQLSTE-QAVLQESLEKE 1216
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEkEAVIEEELDEE 1788
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
980-1127 |
7.46e-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: 41.84 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 980 KARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYE----KLRDtyiEEAEKYKM--QLQEQFDNLNAAHETSKLEIEA 1053
Cdd:pfam08614 20 EAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEqllaQLRE---ELAELYRSrgELAQRLVDLNEELQELEKKLRE 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50348611 1054 ShSEKLELLkkayEASLSEIkkghEIEKKSLEDLLSEKQesleKQINDLKSENDALNEKLKSEEQKRRAREKAN 1127
Cdd:pfam08614 97 D-ERRLAAL----EAERAQL----EEKLKDREEELREKR----KLNQDLQDELVALQLQLNMAEEKLRKLEKEN 157
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1048-1166 |
7.68e-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: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1048 KLEIEASHSEKLELlkkayEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSE----EQKRRAR 1123
Cdd:COG0542 403 RMEIDSKPEELDEL-----ERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEkeliEEIQELK 477
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50348611 1124 EKANLKNPQIMYLEQELESLKAVLEIKNEKLHQ----QDI---------------------KLMKMEK 1166
Cdd:COG0542 478 EELEQRYGKIPELEKELAELEEELAELAPLLREevteEDIaevvsrwtgipvgkllegereKLLNLEE 545
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
944-1230 |
8.51e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 944 LSEREEALKQHKTLSQELVNLRGEL-VTASTTCEKLEKARNELQTVYEAF-VQQ------HQA----EKTERENRLKEFy 1011
Cdd:PRK04863 357 LEELEERLEEQNEVVEEADEQQEENeARAEAAEEEVDELKSQLADYQQALdVQQtraiqyQQAvqalERAKQLCGLPDL- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1012 trEYEKLRDtYIEEaekYKMQLQEQFDNLNAAHEtsKLEIEASHSEKLEllkKAYEASLS-----EIKKGHEIEKKSLED 1086
Cdd:PRK04863 436 --TADNAED-WLEE---FQAKEQEATEELLSLEQ--KLSVAQAAHSQFE---QAYQLVRKiagevSRSEAWDVARELLRR 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1087 LlsEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQdiklmkMEK 1166
Cdd:PRK04863 505 L--REQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES------VSE 576
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50348611 1167 LVDNNTALVDKLKRFQQENEELKAR----MDKHMAISR-------QLSTEQAV---LQESLEKEskvnKRLSMENEEL 1230
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLAARapawLAAQDALARlreqsgeEFEDSQDVteyMQQLLERE----RELTVERDEL 650
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
976-1223 |
8.91e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 976 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEKYKmQLQEQFDNLNAAHETSKLEIEASH 1055
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK-AEEAKKAD-EAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1056 SEklELLKKAYEASLS-EIKKGHEIEKKSLEDLlsEKQESLEKQINDL-KSENDALNEKLKSEEQKRRARE--KA-NLKN 1130
Cdd:PTZ00121 1472 AD--EAKKKAEEAKKAdEAKKKAEEAKKKADEA--KKAAEAKKKADEAkKAEEAKKADEAKKAEEAKKADEakKAeEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1131 PQIMYLEQELESLKAVLEIKNEKLHQQD--IKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHmaisrqlSTEQAV 1208
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDknMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK-------AEEAKI 1620
|
250
....*....|....*
gi 50348611 1209 LQESLEKESKVNKRL 1223
Cdd:PTZ00121 1621 KAEELKKAEEEKKKV 1635
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
977-1230 |
9.32e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.91 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 977 KLEKARNELQTVYEAFVQQHQAEKTERENR---LKEFYTREYEKLRDTYIEEaeKYKMQLQEQFDNLNAAHETSKLEIEA 1053
Cdd:COG5022 814 SYLACIIKLQKTIKREKKLRETEEVEFSLKaevLIQKFGRSLKAKKRFSLLK--KETIYLQSAQRVELAERQLQELKIDV 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1054 SHSEKLELLKKAYEASLSEIKKgheiekkSLEDLLSEKqeslekqiNDLKSENDALNEKLKSEEQKRRAREKANLKNPQI 1133
Cdd:COG5022 892 KSISSLKLVNLELESEIIELKK-------SLSSDLIEN--------LEFKTELIARLKKLLNNIDLEEGPSIEYVKLPEL 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1134 MYLEQELESLKAVLEIKNEKLHQQDI-------KLMKMEKLVDNNTALVDKLKRFQQENEELKARMDK---HMAISRQLS 1203
Cdd:COG5022 957 NKLHEVESKLKETSEEYEDLLKKSTIlvregnkANSELKNFKKELAELSKQYGALQESTKQLKELPVEvaeLQSASKIIS 1036
|
250 260
....*....|....*....|....*..
gi 50348611 1204 TEQAVLQeSLEKESKVNKRLSMENEEL 1230
Cdd:COG5022 1037 SESTELS-ILKPLQKLKGLLLLENNQL 1062
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
955-1229 |
1.07e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.67 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 955 KTLSQELVNLRGELVtasttcEKLEKARNELQTvyEAFVQQHqaEKTERENRLKEFYTREYEKLRDTYIEEaekYKMQLQ 1034
Cdd:PTZ00440 896 KQLVEHLLNNKIDLK------NKLEQHMKIINT--DNIIQKN--EKLNLLNNLNKEKEKIEKQLSDTKINN---LKMQIE 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1035 EQFDnlnaAHETSKLEIEA---SHSEKLELLKKAYEASLSEIKK---GHEIEKKSLEDLLSE-KQESLEKQINDLKSEND 1107
Cdd:PTZ00440 963 KTLE----YYDKSKENINGndgTHLEKLDKEKDEWEHFKSEIDKlnvNYNILNKKIDDLIKKqHDDIIELIDKLIKEKGK 1038
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1108 ALNEKLKSeeqkrrarekanlknpQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEE 1187
Cdd:PTZ00440 1039 EIEEKVDQ----------------YISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIE 1102
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 50348611 1188 LKARMDKHMAISRQLSTEQAVL----QESLEK-----ESKVNKRLSMENEE 1229
Cdd:PTZ00440 1103 IKNKSHEHVVNADKEKNKQTEHynkkKKSLEKiykqmEKTLKELENMNLED 1153
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
990-1215 |
1.09e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 990 EAFVQQHQAEKT---ERENRLKEFYtREYEKLRDTYIEEAEKYKM--QLQEQFDNLNAAHET-SKLEIEASH------SE 1057
Cdd:COG4913 210 DDFVREYMLEEPdtfEAADALVEHF-DDLERAHEALEDAREQIELlePIRELAERYAAARERlAELEYLRAAlrlwfaQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1058 KLELLKKAYEASLSEIKKgHEIEKKSLEDLLSEKQESLE-----------KQINDLKSENDALNEKLkseEQKRRAREKa 1126
Cdd:COG4913 289 RLELLEAELEELRAELAR-LEAELERLEARLDALREELDeleaqirgnggDRLEQLEREIERLEREL---EERERRRAR- 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1127 nlknpqimyLEQELESLKavLEIKNEKlhqqdiklmkmEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQ 1206
Cdd:COG4913 364 ---------LEALLAALG--LPLPASA-----------EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
250
....*....|..
gi 50348611 1207 AVLQ---ESLEK 1215
Cdd:COG4913 422 RELEaeiASLER 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
903-1124 |
1.14e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 903 LELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELvtasttcEKLEKAR 982
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL-------EKLKREI 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 983 NELQtvyeafvqqhqaekterenrlkefytREYEKLRDTyieeaekyKMQLQEQFDNLNAAHETSKLEIEASHSEKLELL 1062
Cdd:TIGR02169 402 NELK--------------------------RELDRLQEE--------LQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50348611 1063 K--KAYEASLSEIKKGHEIEKKSLEDlLSEKQESLEKQINDLKSENDALneklksEEQKRRARE 1124
Cdd:TIGR02169 448 LeiKKQEWKLEQLAADLSKYEQELYD-LKEEYDRVEKELSKLQRELAEA------EAQARASEE 504
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
940-1158 |
1.57e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 940 IQHLLSEREEALKQHKTLSQELVNLRGELVTASttcEKLEKARNELQTVyEAFVQQHQAEKTERENRLKEFYtreyeklr 1019
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELN---EEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERR-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1020 dtyieeaEKYKMQLQEQFDNLNAaheTSKLE-IEASHS-----EKLELLKKAYEASLSEIKkgheiEKKSLEDLLSEKQE 1093
Cdd:COG3883 86 -------EELGERARALYRSGGS---VSYLDvLLGSESfsdflDRLSALSKIADADADLLE-----ELKADKAELEAKKA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50348611 1094 SLEKQINDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQD 1158
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAElEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
916-1242 |
1.64e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 916 SGFILQLKQLLACGNTKFEALTVVIQHL------LSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVY 989
Cdd:TIGR00618 204 QLLTLCTPCMPDTYHERKQVLEKELKHLrealqqTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQ 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 990 EAFVQQHQAEKterenrlkefYTREYEKLrdTYIE-EAEKYKMQLQEQFDNLNAA--HETSKLEIEASHSEKLELLKKAY 1066
Cdd:TIGR00618 284 ERINRARKAAP----------LAAHIKAV--TQIEqQAQRIHTELQSKMRSRAKLlmKRAAHVKQQSSIEEQRRLLQTLH 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1067 EASlSEIKKGHEIEKKSLEDllSEKQESLEKQINDLKSENDALNEKLKSEEQK----RRAREKANLKNPQIMYLEQELES 1142
Cdd:TIGR00618 352 SQE-IHIRDAHEVATSIREI--SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEldilQREQATIDTRTSAFRDLQGQLAH 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1143 LKAVLEIKNEKLHQQDIKLMK-MEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNK 1221
Cdd:TIGR00618 429 AKKQQELQQRYAELCAAAITCtAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCG 508
|
330 340
....*....|....*....|.
gi 50348611 1222 RLSMENEELLWKLHNGDLCSP 1242
Cdd:TIGR00618 509 SCIHPNPARQDIDNPGPLTRR 529
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
904-1187 |
2.07e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 904 ELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHllsereeALKQHKTLSQELVNLRGELVTASTTCEKLEKARN 983
Cdd:PRK01156 191 KLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNN-------AMDDYNNLKSALNELSSLEDMKNRYESEIKTAES 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 984 ELQTVYEAFVQQhqAEKTERENRL---KEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKleieashseKLE 1060
Cdd:PRK01156 264 DLSMELEKNNYY--KELEERHMKIindPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIK---------KLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1061 LLKKAYEAslseikkgHEIEKKSLEDLlsekqeslEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQI-MYLEQE 1139
Cdd:PRK01156 333 VLQKDYND--------YIKKKSRYDDL--------NNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMsAFISEI 396
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 50348611 1140 LESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEE 1187
Cdd:PRK01156 397 LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSR 444
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1047-1227 |
2.11e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1047 SKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLE---KQINDLKSENDALNEKLKS-EEQKRRA 1122
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEqarEELEQLEEELEQARSELEQlEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1123 REKANLKNPQIMYLEQELESLKAvleiKNEKLHQQdiklmkMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQL 1202
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQE----EAEELQEE------LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180
....*....|....*....|....*
gi 50348611 1203 STEQAVLQESLEKESKVNKRLSMEN 1227
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAE 180
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
940-1230 |
2.39e-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: 42.25 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 940 IQHLLSEREEALKQHKT----LSQELVNLRG-----ELVTASTTCEKLEKARNELQTVYEA--FVQQHQaektereNRLk 1008
Cdd:COG3096 848 LERELAQHRAQEQQLRQqldqLKEQLQLLNKllpqaNLLADETLADRLEELREELDAAQEAqaFIQQHG-------KAL- 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1009 efytREYEKLRDTyieeaekykmqLQ---EQFDNLNAAHETSKleieashsEKLELLKKAYEAsLSEIKKgheiekkSLE 1085
Cdd:COG3096 920 ----AQLEPLVAV-----------LQsdpEQFEQLQADYLQAK--------EQQRRLKQQIFA-LSEVVQ-------RRP 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1086 DLLSEKQESLEKQINDLkseNDALNEKLKSEEQKR-RAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKM 1164
Cdd:COG3096 969 HFSYEDAVGLLGENSDL---NEKLRARLEQAEEARrEAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL 1045
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1165 EKLVDNNTAlvdklKRFQQENEELKARMDKHMAISRQLSTEQAVL---QESLEKE-SKVNKRLSMENEEL 1230
Cdd:COG3096 1046 GVQADAEAE-----ERARIRRDELHEELSQNRSRRSQLEKQLTRCeaeMDSLQKRlRKAERDYKQEREQV 1110
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
940-1145 |
2.51e-03 |
|
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: 40.82 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 940 IQHLLSEREEALKQhktLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAfvQQHQAEKteRENRLKEFYTREYEKLR 1019
Cdd:pfam04012 13 IHEGLDKAEDPEKM---LEQAIRDMQSELVKARQALAQTIARQKQLERRLEQ--QTEQAKK--LEEKAQAALTKGNEELA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1020 DTYIEEAEKYKMQ---LQEQFDNLNAAHETSKLEIEASHS--EKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQES 1094
Cdd:pfam04012 86 REALAEKKSLEKQaeaLETQLAQQRSAVEQLRKQLAALETkiQQLKAKKNLLKARLKAAKAQEAVQTSLGSLSTSSATDS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 50348611 1095 LEK---QINDLKSENDALNE--KLKSEEQKRRArEKANLKNPqimylEQELESLKA 1145
Cdd:pfam04012 166 FERieeKIEEREARADAAAElaSAVDLDAKLEQ-AGIQMEVS-----EDVLARLKA 215
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
921-1065 |
2.99e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 921 QLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTC------EKLEKARNELQTVYEAfVQ 994
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeeeleEELEELEEELEELEEE-LE 449
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50348611 995 QHQAEKTERENRLKEFYT-REYEKLRDTYIEEAEKYKmQLQEQFDNLNAAHETSKLEIEASHSEKL-ELLKKA 1065
Cdd:COG4717 450 ELREELAELEAELEQLEEdGELAELLQELEELKAELR-ELAEEWAALKLALELLEEAREEYREERLpPVLERA 521
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
976-1156 |
3.78e-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: 41.06 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 976 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYE-KLRDTYIEEAEKYKMQLQEqfdnLNAAHETSKLEIEAS 1054
Cdd:pfam13868 176 EEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQErKERQKEREEAEKKARQRQE----LQQAREEQIELKERR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1055 HSEKLELLKKAYEASLSEIKKGHEIEKKSLED---LLSEKQESLEKQINdlksendalneklksEEQKRRAREKANLKNP 1131
Cdd:pfam13868 252 LAEEAEREEEEFERMLRKQAEDEEIEQEEAEKrrmKRLEHRRELEKQIE---------------EREEQRAAEREEELEE 316
|
170 180
....*....|....*....|....*
gi 50348611 1132 QIMYLEQELESLKAVLEIKNEKLHQ 1156
Cdd:pfam13868 317 GERLREEEAERRERIEEERQKKLKE 341
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
944-1156 |
3.98e-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: 40.12 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 944 LSEREEALKQHKTLSQELVNLRGELvtasttceklekarNELQTVYEAFVQQHQAEKTERENRLKEFyTREYEKLRDTYI 1023
Cdd:cd00176 32 LESVEALLKKHEALEAELAAHEERV--------------EALNELGEQLIEEGHPDAEEIQERLEEL-NQRWEELRELAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1024 EEAEKYK--MQLQEQFDNLnaahetskLEIEASHSEKlellkkayEASLSEIKKGHEIEkkSLEDLLsEKQESLEKQIND 1101
Cdd:cd00176 97 ERRQRLEeaLDLQQFFRDA--------DDLEQWLEEK--------EAALASEDLGKDLE--SVEELL-KKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 50348611 1102 LKSENDALNEKLKSEEQKRRAREKANLKNPQIMyLEQELESLKAVLEIKNEKLHQ 1156
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEE-LNERWEELLELAEERQKKLEE 211
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
978-1228 |
4.48e-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: 41.58 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 978 LEKARNELQTVyeafVQQHQAEKTERENRLKEFYTR---EYEKLRdtyieeaekykmqlqeqfdnlNAAHETSKLEIEAS 1054
Cdd:TIGR01612 673 IDALYNELSSI----VKENAIDNTEDKAKLDDLKSKidkEYDKIQ---------------------NMETATVELHLSNI 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1055 HSEKLELLkkayeASLSEIKKG--HEIEK---KSLEDLLSeKQESLEKQINDLKSENDALNE-KLKSEEQKRRAREKANL 1128
Cdd:TIGR01612 728 ENKKNELL-----DIIVEIKKHihGEINKdlnKILEDFKN-KEKELSNKINDYAKEKDELNKyKSKISEIKNHYNDQINI 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1129 KNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEE-LKARMDKHMAISRQLSTEqa 1207
Cdd:TIGR01612 802 DNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEkIDSEHEQFAELTNKIKAE-- 879
|
250 260
....*....|....*....|..
gi 50348611 1208 VLQESLEK-ESKVNKRLSMENE 1228
Cdd:TIGR01612 880 ISDDKLNDyEKKFNDSKSLINE 901
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
947-1218 |
4.48e-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: 41.10 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 947 REEALKQHKTLSQELVNLRGELVTA-STTCEKLE--KARNELQTVYEAFVQQHQA--EKTERENRLKEFYT------REY 1015
Cdd:COG5185 266 RLEKLGENAESSKRLNENANNLIKQfENTKEKIAeyTKSIDIKKATESLEEQLAAaeAEQELEESKRETETgiqnltAEI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1016 EKLRDTYIEEAEKYKM------------QLQEQFDNLNAAHETSKLEIEASH---SEKLELLKKAYEASLSEIKKGHEIE 1080
Cdd:COG5185 346 EQGQESLTENLEAIKEeienivgevelsKSSEELDSFKDTIESTKESLDEIPqnqRGYAQEILATLEDTLKAADRQIEEL 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1081 KKSLEDLLSEKQES------LEKQINDLKSENDALNEKLKSEEQK---RRAREKANLKNPQIMYLEQELESLKAVLEIKN 1151
Cdd:COG5185 426 QRQIEQATSSNEEVskllneLISELNKVMREADEESQSRLEEAYDeinRSVRSKKEDLNEELTQIESRVSTLKATLEKLR 505
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50348611 1152 EKLHQQdikLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESK 1218
Cdd:COG5185 506 AKLERQ---LEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAV 569
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
1058-1166 |
4.48e-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: 38.32 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1058 KLELLKKAYEASLSEIKKgheiekksLEDLLSEKQESLEKQINDLKSENDALNEKLK-SEEQKRRAREKANLKNPQIMYL 1136
Cdd:pfam13863 7 EMFLVQLALDAKREEIER--------LEELLKQREEELEKKEQELKEDLIKFDKFLKeNDAKRRRALKKAEEETKLKKEK 78
|
90 100 110
....*....|....*....|....*....|
gi 50348611 1137 EQELESLKAVLEIKNEKLHQQDIKLMKMEK 1166
Cdd:pfam13863 79 EKEIKKLTAQIEELKSEISKLEEKLEEYKP 108
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
959-1218 |
4.66e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 41.28 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 959 QELVNLRGELVTASTTCEKlEKARNELQTV-YEAFVQQHQAEKTERENRLKEFYTREY--EKLRDTYIEEAEKYKMQLQE 1035
Cdd:pfam07111 73 QELRRLEEEVRLLRETSLQ-QKMRLEAQAMeLDALAVAEKAGQAEAEGLRAALAGAEMvrKNLEEGSQRELEEIQRLHQE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1036 QFDNLNAAHETSkLEIEASHSEKLELLKKAYEASLS-EIKKGHEIEKKS--LEDLLSEKQESLEKQINDLKSENDALNEK 1112
Cdd:pfam07111 152 QLSSLTQAHEEA-LSSLTSKAEGLEKSLNSLETKRAgEAKQLAEAQKEAelLRKQLSKTQEELEAQVTLVESLRKYVGEQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1113 LKSE------EQKRRA---------REKANLKnPQIMYLEQELESLKAVLEIKNEKLHQqdiKLMKMEKLVDNNTALVDK 1177
Cdd:pfam07111 231 VPPEvhsqtwELERQElldtmqhlqEDRADLQ-ATVELLQVRVQSLTHMLALQEEELTR---KIQPSDSLEPEFPKKCRS 306
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 50348611 1178 LKRFQQENE-----ELKARMDKHMAISRQLSTEQAVLQESLEKESK 1218
Cdd:pfam07111 307 LLNRWREKVfalmvQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQ 352
|
|
| Ctf13_LRR_LRR-insertion |
cd19611 |
leucine-rich-repeat (LRR) domain and LRR insertion domain of centromere DNA-binding protein ... |
1069-1156 |
4.85e-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: 40.40 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1069 SLSEIKK-GHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLK--A 1145
Cdd:cd19611 14 NPNMVKKiLKVLEKKELLDLVSEVFFGQDEEESDEEDEDDSSKNDRKKLTDDDVKEKSYKLNDPSIIRIISSLESMKnlR 93
|
90
....*....|.
gi 50348611 1146 VLEIKNEKLHQ 1156
Cdd:cd19611 94 KLSVRGDNLYE 104
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1062-1203 |
5.00e-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: 41.58 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1062 LKKAYEASLSEIKKGHEIEKKSLEDllSEKQESLEKQINDLksendaLNEKLKSEEQkrrarekanlkNPQIMYLEQELE 1141
Cdd:TIGR01612 546 LKESYELAKNWKKLIHEIKKELEEE--NEDSIHLEKEIKDL------FDKYLEIDDE-----------IIYINKLKLELK 606
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50348611 1142 SLKAVLEIKNEKLHqqdiKLMKMEKLVDNNTALVDKLKRFQ--QENEELKARMDKHMAISRQLS 1203
Cdd:TIGR01612 607 EKIKNISDKNEYIK----KAIDLKKIIENNNAYIDELAKISpyQVPEHLKNKDKIYSTIKSELS 666
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
931-1126 |
5.01e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 931 TKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeAFVQQHQAEKTERENRLKEF 1010
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ----AEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1011 YTREYEKLRD-TYIE---EAEKYKmQLQEQFDNLNAAHETSKLEIEASHSEKLELlkKAYEASLSEIKKGHEIEKKSLED 1086
Cdd:COG3883 92 ARALYRSGGSvSYLDvllGSESFS-DFLDRLSALSKIADADADLLEELKADKAEL--EAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 50348611 1087 LLSE---KQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA 1126
Cdd:COG3883 169 AKAEleaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
936-1223 |
5.87e-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: 40.88 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 936 LTVVIQHLLSEREEalkqhkTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTEREnRLKEFYTREY 1015
Cdd:pfam05557 273 LNLRSPEDLSRRIE------QLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLK-RHKALVRRLQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1016 EKLRdTYIEEAEKYKmQLQEQFDNLNAAHETSKLEIEasHSEKLELLKKAYEASLSEIKkgHEIEKkSLEDLLSEKQ--E 1093
Cdd:pfam05557 346 RRVL-LLTKERDGYR-AILESYDKELTMSNYSPQLLE--RIEEAEDMTQKMQAHNEEME--AQLSV-AEEELGGYKQqaQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1094 SLEKQINDLKSENDaLNEKLKSEEQKRRARekanLKNPQIMYLEQELESLKAVLEIKNEKLHQQ---DIKLMKMEKLVDN 1170
Cdd:pfam05557 419 TLERELQALRQQES-LADPSYSKEEVDSLR----RKLETLELERQRLREQKNELEMELERRCLQgdyDPKKTKVLHLSMN 493
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50348611 1171 NTALV-----DKLKRFQQENEELKARMDKHMAISRQLST-----------EQAVLQESLEKESKVNKRL 1223
Cdd:pfam05557 494 PAAEAyqqrkNQLEKLQAEIERLKRLLKKLEDDLEQVLRlpettstmnfkEVLDLRKELESAELKNQRL 562
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
940-1223 |
6.13e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.18 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 940 IQHLLSEREEALKQHKTLSQELVNLRGELVTA-------STTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLkefYT 1012
Cdd:pfam15905 82 IRALVQERGEQDKRLQALEEELEKVEAKLNAAvrektslSASVASLEKQLLELTRVNELLKAKFSEDGTQKKMSS---LS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1013 REYEKLRDTyIEEAEKYKMQLQEqfdnlnaahetsKLEIeashseKLELLKKAYEASLSEIKKgheiekksledlLSEKQ 1092
Cdd:pfam15905 159 MELMKLRNK-LEAKMKEVMAKQE------------GMEG------KLQVTQKNLEHSKGKVAQ------------LEEKL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1093 ESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKnpqIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKlvdnnt 1172
Cdd:pfam15905 208 VSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLD---IAQLEELLKEKNDEIESLKQSLEEKEQELSKQIK------ 278
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 50348611 1173 ALVDKLKRFQQENEELKARmdkHMAISRQLSTEQAVLQESLEKESKVNKRL 1223
Cdd:pfam15905 279 DLNEKCKLLESEKEELLRE---YEEKEQTLNAELEELKEKLTLEEQEHQKL 326
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
978-1188 |
6.14e-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: 39.66 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 978 LEKARNELQTV-YEAFVQQHQAEKTERENRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLnaahetsKLEIEASHS 1056
Cdd:pfam05010 10 LEKARNEIEEKeLEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKV-------LEEKDQALA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1057 EKLELlkkayEASLSEIKKGHEIEKKSLEDlLSEKQESLEKQINDLKsendalnEKLKSEEQ-----KRRAREKANLKNP 1131
Cdd:pfam05010 83 DLNSV-----EKSFSDLFKRYEKQKEVISG-YKKNEESLKKCAQDYL-------ARIKKEEQryqalKAHAEEKLDQANE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 50348611 1132 QIMYLEQELESLKAVLEIkneKLHQQDIKLMKMEKLVDNNTalvdklkrfqQENEEL 1188
Cdd:pfam05010 150 EIAQVRSKAKAETAALQA---SLRKEQMKVQSLERQLEQKT----------KENEEL 193
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
994-1139 |
6.97e-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: 40.71 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 994 QQHQAEKTERENRLKEFYTREYEK------LRDTYIE------EAEKYKMQLQEQfdnlnAAHETSKLEIEASHSEKLEL 1061
Cdd:pfam15709 361 RRLQQEQLERAEKMREELELEQQRrfeeirLRKQRLEeerqrqEEEERKQRLQLQ-----AAQERARQQQEEFRRKLQEL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1062 LKKAYEASLsEIKKGHEIEKKSLEDLLSEKQ---------ESLEKQINDLKSENDAlneKLKSEEQKRRAREKANLKNPQ 1132
Cdd:pfam15709 436 QRKKQQEEA-ERAEAEKQRQKELEMQLAEEQkrlmemaeeERLEYQRQKQEAEEKA---RLEAEERRQKEEEAARLALEE 511
|
....*..
gi 50348611 1133 IMYLEQE 1139
Cdd:pfam15709 512 AMKQAQE 518
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
931-1234 |
7.44e-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: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 931 TKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeafvQQHQAEKTERENRLKEF 1010
Cdd:pfam01576 636 TRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALE-------QQVEEMKTQLEELEDEL 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1011 YTREYEKLR----------------DTYIEEAEKYKMQLQEQFDNLNAAHETSKLE--IEASHSEKLELLKKAYEASLSE 1072
Cdd:pfam01576 709 QATEDAKLRlevnmqalkaqferdlQARDEQGEEKRRQLVKQVRELEAELEDERKQraQAVAAKKKLELDLKELEAQIDA 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1073 IKKGHEIEKKSLEDLLSEKQEsLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpQIMYLEQEL---ESLKAVLEI 1149
Cdd:pfam01576 789 ANKGREEAVKQLKKLQAQMKD-LQRELEEARASRDEILAQSKESEKKLKNLEA------ELLQLQEDLaasERARRQAQQ 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1150 KNEKLhQQDIK--LMKMEKLVDNNTALVDKLKRFQQENEE-------LKARMDKHMAISRQLSTEQAVLQESLEKESKVN 1220
Cdd:pfam01576 862 ERDEL-ADEIAsgASGKSALQDEKRRLEARIAQLEEELEEeqsntelLNDRLRKSTLQVEQLTTELAAERSTSQKSESAR 940
|
330
....*....|....
gi 50348611 1221 KRLSMENEELLWKL 1234
Cdd:pfam01576 941 QQLERQNKELKAKL 954
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1057-1171 |
7.48e-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: 40.00 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1057 EKLELLKKAYEaslsEIKKgHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQkrRAREKANLKNPQIMY- 1135
Cdd:smart00787 151 ENLEGLKEDYK----LLMK-ELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELD--RAKEKLKKLLQEIMIk 223
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 50348611 1136 ------LEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNN 1171
Cdd:smart00787 224 vkkleeLEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQC 265
|
|
| PRK14160 |
PRK14160 |
heat shock protein GrpE; Provisional |
1080-1194 |
7.81e-03 |
|
heat shock protein GrpE; Provisional
Pssm-ID: 237629 [Multi-domain] Cd Length: 211 Bit Score: 39.35 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348611 1080 EKKSLEDLLSEKQESLEKQiNDLKSENDALNEKLKSEEQKrrAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQdi 1159
Cdd:PRK14160 2 EKECKDAKHENMEEDCCKE-NENKEEDKGKEEDLEFEEIE--KEEIIEDSEESNEVKIEELKDENNKLKEENKKLENE-- 76
|
90 100 110
....*....|....*....|....*....|....*
gi 50348611 1160 klmkMEklvdnntALVDKLKRFQQENEELKARMDK 1194
Cdd:PRK14160 77 ----LE-------ALKDRLLRTVAEYDNYRKRTAK 100
|
|
| |
